메뉴 건너뛰기




Volumn 35, Issue 1, 2011, Pages 147-200

Fibronectin: A multidomain host adhesin targeted by bacterial fibronectin-binding proteins

Author keywords

Bacterial pathogenesis; Fibronectin; Fibronectin binding proteins

Indexed keywords

ACTIN; ADHESIN; ALPHA INTERFERON; BETA1 INTEGRIN; COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COLLAGEN TYPE 4; CYTOKINE; FIBRIN; FIBRONECTIN; FIBRONECTIN 1; FIBRONECTIN 2; FIBRONECTIN 3; FIBRONECTIN BINDING PROTEIN; FIBULIN; GELATIN; GLYOXYLIC ACID; HEPARIN; HETERODIMER; INTERLEUKIN 6; ISONIAZID; LAMININ; LEUCINE RICH REPEAT KINASE 2; MALATE SYNTHASE; MONOCLONAL ANTIBODY; SYNAPSIN I; TEFIBAZUMAB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VITRONECTIN;

EID: 78650028835     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1111/j.1574-6976.2010.00243.x     Document Type: Article
Times cited : (266)

References (460)
  • 2
    • 0027944178 scopus 로고
    • Human cytomegalovirus interaction with platelets and adhesive glycoproteins
    • J Infect Dis
    • Agbanyo F & Wasi S (1994) Human cytomegalovirus interaction with platelets and adhesive glycoproteins: significance in viral pathogenesis. J Infect Dis 170: 1120-1127.
    • (1994) significance in viral pathogenesis , vol.170 , pp. 1120-1127
    • Agbanyo, F.1    Wasi, S.2
  • 3
    • 0142180077 scopus 로고    scopus 로고
    • Integrin-mediated invasion of Staphylococcus aureus into human cells requires Src family protein tyrosine kinases
    • Agerer F, Michel A, Ohlsen K & Hauck CR (2003) Integrin-mediated invasion of Staphylococcus aureus into human cells requires Src family protein tyrosine kinases. J Biol Chem 278: 42524-42531.
    • (2003) J Biol Chem , vol.278 , pp. 42524-42531
    • Agerer, F.1    Michel, A.2    Ohlsen, K.3    Hauck, C.R.4
  • 4
    • 21044436925 scopus 로고    scopus 로고
    • Cellular invasion by Staphylococcus aureus reveals a functional link between focal adhesion kinase and cortactin in integrin-mediated internalisation
    • Agerer F, Lux S, Michel A, Rohde M, Ohlsen K & Hauck CR (2005) Cellular invasion by Staphylococcus aureus reveals a functional link between focal adhesion kinase and cortactin in integrin-mediated internalisation. J Cell Sci 118: 2189-2200.
    • (2005) J Cell Sci , vol.118 , pp. 2189-2200
    • Agerer, F.1    Lux, S.2    Michel, A.3    Rohde, M.4    Ohlsen, K.5    Hauck, C.R.6
  • 5
    • 0035055294 scopus 로고    scopus 로고
    • Staphylococcus aureus fibronectin binding proteins are essential for internalization by osteoblasts but do not account for differences in intracellular levels of bacteria
    • Ahmed S, Meghji S, Williams RJ, Henderson B, Brock JH & Nair SP (2001) Staphylococcus aureus fibronectin binding proteins are essential for internalization by osteoblasts but do not account for differences in intracellular levels of bacteria. Infect Immun 69: 2872-2877.
    • (2001) Infect Immun , vol.69 , pp. 2872-2877
    • Ahmed, S.1    Meghji, S.2    Williams, R.J.3    Henderson, B.4    Brock, J.H.5    Nair, S.P.6
  • 6
    • 0019161425 scopus 로고
    • Surface characterization of virulent Treponema pallidum
    • Alderete JF & Baseman JB (1980) Surface characterization of virulent Treponema pallidum. Infect Immun 30: 814-823.
    • (1980) Infect Immun , vol.30 , pp. 814-823
    • Alderete, J.F.1    Baseman, J.B.2
  • 7
    • 0017724384 scopus 로고
    • Effect of cytochalasin B and colchicines on the attachment of a major surface protein of fibroblasts
    • Ali IU & Hynes RO (1977) Effect of cytochalasin B and colchicines on the attachment of a major surface protein of fibroblasts. Biochim Biophys Acta 471: 16-24.
    • (1977) Biochim Biophys Acta , vol.471 , pp. 16-24
    • Ali, I.U.1    Hynes, R.O.2
  • 8
    • 0018143325 scopus 로고
    • Role of disulfide bonds in the attachment and function of large, external transformation-sensitive glycoprotein at the cell surface
    • Ali IU & Hynes RO (1978) Role of disulfide bonds in the attachment and function of large, external transformation-sensitive glycoprotein at the cell surface. Biochim Biophys Acta 510: 140-150.
    • (1978) Biochim Biophys Acta , vol.510 , pp. 140-150
    • Ali, I.U.1    Hynes, R.O.2
  • 9
    • 0017646305 scopus 로고
    • Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein
    • Ali IU, Mautner VM, Lanza RP & Hynes RO (1977) Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell 11: 115-126.
    • (1977) Cell , vol.11 , pp. 115-126
    • Ali, I.U.1    Mautner, V.M.2    Lanza, R.P.3    Hynes, R.O.4
  • 10
    • 0037031133 scopus 로고    scopus 로고
    • Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding
    • Allignet J, England P, Old I & El Solh N (2001) Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding. FEMS Microbiol Lett 213: 193-197.
    • (2001) FEMS Microbiol Lett , vol.213 , pp. 193-197
    • Allignet, J.1    England, P.2    Old, I.3    El Solh, N.4
  • 12
    • 0035937258 scopus 로고    scopus 로고
    • An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (antigen 85B), a mycolyl transferase
    • Anderson DH, Harth G, Horwitz MA & Eisenberg D (2001) An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (antigen 85B), a mycolyl transferase. J Mol Biol 307: 671-681.
    • (2001) J Mol Biol , vol.307 , pp. 671-681
    • Anderson, D.H.1    Harth, G.2    Horwitz, M.A.3    Eisenberg, D.4
  • 13
    • 48749086405 scopus 로고    scopus 로고
    • Vaccination with clumping factor A and fibronectin binding protein A to prevent Staphylococcus aureus infection of an aortic patch in mice
    • Arrecubieta C, Matsunaga I, Asai T, Naka Y, Deng MC & Lowy FD (2008) Vaccination with clumping factor A and fibronectin binding protein A to prevent Staphylococcus aureus infection of an aortic patch in mice. J Infect Dis 198: 571-575.
    • (2008) J Infect Dis , vol.198 , pp. 571-575
    • Arrecubieta, C.1    Matsunaga, I.2    Asai, T.3    Naka, Y.4    Deng, M.C.5    Lowy, F.D.6
  • 15
    • 0025237471 scopus 로고
    • Signal transduction for chemotaxis and haptotaxis by matrix molecules in tumour cells
    • Aznavoorian S, Stracke ML, Krutzsch H, Schiffmann E & Liotta LA (1990) Signal transduction for chemotaxis and haptotaxis by matrix molecules in tumour cells. J Cell Biol 110: 1427-1438.
    • (1990) J Cell Biol , vol.110 , pp. 1427-1438
    • Aznavoorian, S.1    Stracke, M.L.2    Krutzsch, H.3    Schiffmann, E.4    Liotta, L.A.5
  • 16
    • 46449125693 scopus 로고    scopus 로고
    • The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin
    • Balasubramanian S, Kannan TR & Baseman JB (2008) The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin. Infect Immun 76: 3116-3123.
    • (2008) Infect Immun , vol.76 , pp. 3116-3123
    • Balasubramanian, S.1    Kannan, T.R.2    Baseman, J.B.3
  • 17
    • 0021116807 scopus 로고
    • Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator
    • Bányai L, Váradi A & Patthy L (1983) Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator. FEBS Lett 163: 37-41.
    • (1983) FEBS Lett , vol.163 , pp. 37-41
    • Bányai, L.1    Váradi, A.2    Patthy, L.3
  • 19
    • 0025337477 scopus 로고
    • Structure of the fibronectin type 1 module
    • Baron M, Norman D, Willis A & Campbell ID (1990) Structure of the fibronectin type 1 module. Nature 345: 642-646.
    • (1990) Nature , vol.345 , pp. 642-646
    • Baron, M.1    Norman, D.2    Willis, A.3    Campbell, I.D.4
  • 20
    • 0028804043 scopus 로고
    • Bartonella henselae and Bartonella quintana adherence to and entry into cultured human epithelial cells
    • Batterman HJ, Peek JA, Loutit JS, Falkow S & Tompkins LS (1995) Bartonella henselae and Bartonella quintana adherence to and entry into cultured human epithelial cells. Infect Immun 63: 4553-4556.
    • (1995) Infect Immun , vol.63 , pp. 4553-4556
    • Batterman, H.J.1    Peek, J.A.2    Loutit, J.S.3    Falkow, S.4    Tompkins, L.S.5
  • 21
    • 0032925381 scopus 로고    scopus 로고
    • Binding of Haemophilus ducreyi to extracellular matrix proteins
    • Bauer ME & Spinola SM (1999) Binding of Haemophilus ducreyi to extracellular matrix proteins. Infect Immun 67: 2649-2652.
    • (1999) Infect Immun , vol.67 , pp. 2649-2652
    • Bauer, M.E.1    Spinola, S.M.2
  • 22
    • 0029959349 scopus 로고    scopus 로고
    • Molecular mimicry between an immunodominant amino acid motif on the 47kDa lipoprotein of Treponema pallidum (Tpp47) and multiple repeats of analogous sequences in fibronectin
    • Baughn RE, Jiang A, Abraham R, Ottmers V & Musher DM (1996) Molecular mimicry between an immunodominant amino acid motif on the 47kDa lipoprotein of Treponema pallidum (Tpp47) and multiple repeats of analogous sequences in fibronectin. J Immunol 157: 720-731.
    • (1996) J Immunol , vol.157 , pp. 720-731
    • Baughn, R.E.1    Jiang, A.2    Abraham, R.3    Ottmers, V.4    Musher, D.M.5
  • 23
    • 33750481888 scopus 로고    scopus 로고
    • Identification of a novel virulence determinant with serum opacification activity in Streptococcus suis
    • Baums CG, Kaim U, Fulde M, Ramachandran G, Goethe R & Valentin-Weigand P (2006) Identification of a novel virulence determinant with serum opacification activity in Streptococcus suis. Infect Immun 74: 6154-6162.
    • (2006) Infect Immun , vol.74 , pp. 6154-6162
    • Baums, C.G.1    Kaim, U.2    Fulde, M.3    Ramachandran, G.4    Goethe, R.5    Valentin-Weigand, P.6
  • 24
    • 0036266052 scopus 로고    scopus 로고
    • Identification of novel adhesins from Group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding
    • Beckmann C, Waggoner JD, Harris TO, Tamura GS & Rubens CE (2002) Identification of novel adhesins from Group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding. Infect Immun 70: 2869-2876.
    • (2002) Infect Immun , vol.70 , pp. 2869-2876
    • Beckmann, C.1    Waggoner, J.D.2    Harris, T.O.3    Tamura, G.S.4    Rubens, C.E.5
  • 25
    • 0026546935 scopus 로고
    • Fibronectin fragments stimulate tumor necrosis factor secretion by human monocytes
    • Beezhold DH & Personius C (1992) Fibronectin fragments stimulate tumor necrosis factor secretion by human monocytes. J Leukoc Biol 51: 59-64.
    • (1992) J Leukoc Biol , vol.51 , pp. 59-64
    • Beezhold, D.H.1    Personius, C.2
  • 29
    • 23844541986 scopus 로고    scopus 로고
    • Monocytes stimulated by 110-kDa fibronectin fragments suppress proliferation of anti-CD3-activated T cells
    • Birdsall HH, Porter WJ, Trial J & Rossen RD (2005) Monocytes stimulated by 110-kDa fibronectin fragments suppress proliferation of anti-CD3-activated T cells. J Immunol 175: 3347-3353.
    • (2005) J Immunol , vol.175 , pp. 3347-3353
    • Birdsall, H.H.1    Porter, W.J.2    Trial, J.3    Rossen, R.D.4
  • 30
    • 46349112181 scopus 로고    scopus 로고
    • A new adhesin of enteroaggregative Escherichia coli related to the Afa/Dr/AAF family
    • Bolsen N, Struve C, Sheutz F, Krogfelt KA & Nataro JP (2008) A new adhesin of enteroaggregative Escherichia coli related to the Afa/Dr/AAF family. Infect Immun 76: 3281-3292.
    • (2008) Infect Immun , vol.76 , pp. 3281-3292
    • Bolsen, N.1    Struve, C.2    Sheutz, F.3    Krogfelt, K.A.4    Nataro, J.P.5
  • 31
  • 32
    • 0032484685 scopus 로고    scopus 로고
    • Isolation, sequencing and expression of the gene encoding a major protein from the bacteriophage associated with Bartonella henselae
    • Bowers TJ, Sweger D, Jue D & Anderson B (1998) Isolation, sequencing and expression of the gene encoding a major protein from the bacteriophage associated with Bartonella henselae. Gene 206: 49-52.
    • (1998) Gene , vol.206 , pp. 49-52
    • Bowers, T.J.1    Sweger, D.2    Jue, D.3    Anderson, B.4
  • 35
    • 0042235309 scopus 로고    scopus 로고
    • Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors
    • Briknarova K, Akerman NE, Hoyt DW, Ruoslahti E & Ely KR (2003) Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors. J Mol Biol 332: 205-215.
    • (2003) J Mol Biol , vol.332 , pp. 205-215
    • Briknarova, K.1    Akerman, N.E.2    Hoyt, D.W.3    Ruoslahti, E.4    Ely, K.R.5
  • 38
    • 0029139185 scopus 로고
    • Characterization of protein involvement in rabies virus binding to BHK-21 cells
    • Broughan J & Wunner W (1995) Characterization of protein involvement in rabies virus binding to BHK-21 cells. Arch Virol 140: 75-93.
    • (1995) Arch Virol , vol.140 , pp. 75-93
    • Broughan, J.1    Wunner, W.2
  • 39
    • 0041386346 scopus 로고    scopus 로고
    • In vivo and in vitro demonstration that Staphylococcus aureus is an intracelluar pathogen in the presence or absence of fibronectin binding proteins
    • Brouillette E, Grondin G, Shkreta L, Lacasse P & Talbot BG (2003) In vivo and in vitro demonstration that Staphylococcus aureus is an intracelluar pathogen in the presence or absence of fibronectin binding proteins. Microb Pathog 35: 159-168.
    • (2003) Microb Pathog , vol.35 , pp. 159-168
    • Brouillette, E.1    Grondin, G.2    Shkreta, L.3    Lacasse, P.4    Talbot, B.G.5
  • 41
    • 29144442497 scopus 로고    scopus 로고
    • Functional analysis of putative adhesion factors in Lactobacillus acidophilus NCFM
    • Buck BL, Altermann E, Svingerud T & Klaenhammer TR (2005) Functional analysis of putative adhesion factors in Lactobacillus acidophilus NCFM. Appl Environ Microb 71: 8344-8351.
    • (2005) Appl Environ Microb , vol.71 , pp. 8344-8351
    • Buck, B.L.1    Altermann, E.2    Svingerud, T.3    Klaenhammer, T.R.4
  • 42
    • 13844281768 scopus 로고    scopus 로고
    • Sequence analysis and characterization of a novel fibronectin-binding repeat domain from the surface of Streptococcus pneumoniae
    • Bumbaca D, Littlejohn JE, Nayakanti H, Rigden DJ, Galperin MY & Jedrzejas MJ (2004) Sequence analysis and characterization of a novel fibronectin-binding repeat domain from the surface of Streptococcus pneumoniae. OMICS 8: 341-356.
    • (2004) OMICS , vol.8 , pp. 341-356
    • Bumbaca, D.1    Littlejohn, J.E.2    Nayakanti, H.3    Rigden, D.J.4    Galperin, M.Y.5    Jedrzejas, M.J.6
  • 43
    • 0029120352 scopus 로고
    • Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle
    • Busby TF, Argraves WS, Brew SA, Pechik I, Gilliand GL & Ingham KC (1995) Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle. J Biol Chem 270: 18558-18562.
    • (1995) J Biol Chem , vol.270 , pp. 18558-18562
    • Busby, T.F.1    Argraves, W.S.2    Brew, S.A.3    Pechik, I.4    Gilliand, G.L.5    Ingham, K.C.6
  • 44
    • 54549097139 scopus 로고    scopus 로고
    • Streptococcus mutans and Streptococcus intermedius adhesion to fibronectin films are oppositely influenced by ionic strength
    • Busscher HJ, Van De Belt-Gritter B, Dijkstra RJ, Norde W & Van Der Mei HC (2008) Streptococcus mutans and Streptococcus intermedius adhesion to fibronectin films are oppositely influenced by ionic strength. Langmuir 24: 10968-10973.
    • (2008) Langmuir , vol.24 , pp. 10968-10973
    • Busscher, H.J.1    Van De Belt-Gritter, B.2    Dijkstra, R.J.3    Norde, W.4    Van Der Mei, H.C.5
  • 46
    • 0032411670 scopus 로고    scopus 로고
    • Antibody response to fibronectin-binding adhesin FnbpA in patients with Staphylococcus aureus infections
    • Casolini F, Visai L, Joh D, Conaldi PG, Toniolo A, Höök M & Speziale P (1998) Antibody response to fibronectin-binding adhesin FnbpA in patients with Staphylococcus aureus infections. Infect Immun 66: 5433-5442.
    • (1998) Infect Immun , vol.66 , pp. 5433-5442
    • Casolini, F.1    Visai, L.2    Joh, D.3    Conaldi, P.G.4    Toniolo, A.5    Höök, M.6    Speziale, P.7
  • 47
    • 0027477350 scopus 로고
    • Fibronectin cell-binding domain triggered transmembrane signal transduction in human monocytes
    • Chang ZL, Beezhold DH, Personius CD & Shen ZL (1993) Fibronectin cell-binding domain triggered transmembrane signal transduction in human monocytes. J Leukoc Biol 53: 79-85.
    • (1993) J Leukoc Biol , vol.53 , pp. 79-85
    • Chang, Z.L.1    Beezhold, D.H.2    Personius, C.D.3    Shen, Z.L.4
  • 49
    • 0035026419 scopus 로고    scopus 로고
    • ComE, a competence protein from Neisseria gonorrhoeae with DNA-binding activity
    • Chen I & Gotschlich EC (2001) ComE, a competence protein from Neisseria gonorrhoeae with DNA-binding activity. J Bacteriol 183: 3160-3168.
    • (2001) J Bacteriol , vol.183 , pp. 3160-3168
    • Chen, I.1    Gotschlich, E.C.2
  • 50
    • 0036841265 scopus 로고    scopus 로고
    • Immunization with C5a peptidase or peptidase-type III polysaccharide conjugate vaccines enhances clearance of group B streptococci from lungs of infected mice
    • Cheng Q, Debol S, Lam H, Eby R, Edwards L, Matsuka Y, Olmsted SB & Cleary PP (2002a) Immunization with C5a peptidase or peptidase-type III polysaccharide conjugate vaccines enhances clearance of group B streptococci from lungs of infected mice. Infect Immun 70: 6409-6415.
    • (2002) Infect Immun , vol.70 , pp. 6409-6415
    • Cheng, Q.1    Debol, S.2    Lam, H.3    Eby, R.4    Edwards, L.5    Matsuka, Y.6    Olmsted, S.B.7    Cleary, P.P.8
  • 51
    • 0036117970 scopus 로고    scopus 로고
    • The group B streptococcal C5a peptidase is both a specific protease and an invasin
    • Cheng Q, Stafslien D, Purushothaman SS & Cleary P (2002b) The group B streptococcal C5a peptidase is both a specific protease and an invasin. Infect Immun 70: 2408-2413.
    • (2002) Infect Immun , vol.70 , pp. 2408-2413
    • Cheng, Q.1    Stafslien, D.2    Purushothaman, S.S.3    Cleary, P.4
  • 53
    • 33745271833 scopus 로고    scopus 로고
    • Role of fibronectin assembly in platelet thrombus formation
    • Cho J & Mosher DF (2006) Role of fibronectin assembly in platelet thrombus formation. J Thromb Haemost 4: 1461-1469.
    • (2006) J Thromb Haemost , vol.4 , pp. 1461-1469
    • Cho, J.1    Mosher, D.F.2
  • 55
    • 0035987234 scopus 로고    scopus 로고
    • Expression of fibronectin-binding protein FbpA modulates adhesion in Streptococcus gordonii
    • Christie J, McNab R & Jenkinson HF (2002) Expression of fibronectin-binding protein FbpA modulates adhesion in Streptococcus gordonii. Microbiology 148: 1615-1625.
    • (2002) Microbiology , vol.148 , pp. 1615-1625
    • Christie, J.1    McNab, R.2    Jenkinson, H.F.3
  • 56
    • 72949095650 scopus 로고    scopus 로고
    • The giant extracellular matrix-binding protein of Staphylococcus epidermidis mediates biofilm accumulation and attachment to fibronectin
    • Christner M, Franke GC, Schommer NN et al. (2010) The giant extracellular matrix-binding protein of Staphylococcus epidermidis mediates biofilm accumulation and attachment to fibronectin. Mol Microbiol 75: 187-207.
    • (2010) Mol Microbiol , vol.75 , pp. 187-207
    • Christner, M.1    Franke, G.C.2    Schommer, N.N.3
  • 57
    • 0036893408 scopus 로고    scopus 로고
    • Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus
    • Clarke SR, Harris LG, Richards RG & Foster SJ (2002) Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus. Infect Immun 70: 6680-6687.
    • (2002) Infect Immun , vol.70 , pp. 6680-6687
    • Clarke, S.R.1    Harris, L.G.2    Richards, R.G.3    Foster, S.J.4
  • 59
    • 0036839615 scopus 로고    scopus 로고
    • The Haemophilus ducreyi serum resistance antigen DsrA confers attachment to human keratinocytes
    • Cole LE, Kawula TH, Toffer KL & Elkins C (2002) The Haemophilus ducreyi serum resistance antigen DsrA confers attachment to human keratinocytes. Infect Immun 70: 6158-6165.
    • (2002) Infect Immun , vol.70 , pp. 6158-6165
    • Cole, L.E.1    Kawula, T.H.2    Toffer, K.L.3    Elkins, C.4
  • 61
    • 0036199706 scopus 로고    scopus 로고
    • Molecular and cellular basis of the infection by Listeria monocytogenes
    • Int J Med Microbiol
    • Cossart P (2002) Molecular and cellular basis of the infection by Listeria monocytogenes: an overview. Int J Med Microbiol 91: 401-409.
    • (2002) an overview , vol.91 , pp. 401-409
    • Cossart, P.1
  • 63
    • 58349104197 scopus 로고    scopus 로고
    • Bacterial Invasion of Host Cells
    • Lamont RJ, ed) Cambridge University Press, Cambridge.
    • Courtney HS & Podbielski A (2004) Group A streptococcal invasion of host cells. Bacterial Invasion of Host Cells (Lamont RJ, ed), pp. 239-273. Cambridge University Press, Cambridge.
    • (2004) Group A streptococcal invasion of host cells , pp. 239-273
    • Courtney, H.S.1    Podbielski, A.2
  • 64
    • 0026490044 scopus 로고
    • A 28-kilodalton fibronectin-binding protein of group A streptococci
    • Courtney HS, Hasty DL, Dale JB & Poirier TP (1992) A 28-kilodalton fibronectin-binding protein of group A streptococci. Curr Microbiol 25: 245-250.
    • (1992) Curr Microbiol , vol.25 , pp. 245-250
    • Courtney, H.S.1    Hasty, D.L.2    Dale, J.B.3    Poirier, T.P.4
  • 65
    • 0028106317 scopus 로고
    • Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci
    • Courtney HS, Li Y, Dale JB & Hasty DL (1994) Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci. Infect Immun 62: 3937-3946.
    • (1994) Infect Immun , vol.62 , pp. 3937-3946
    • Courtney, H.S.1    Li, Y.2    Dale, J.B.3    Hasty, D.L.4
  • 66
    • 0029945894 scopus 로고    scopus 로고
    • Differential effects of the streptococcal fibronectin binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and Hep-2 tissue culture cells
    • Courtney HS, Dale JB & Hasty DL (1996) Differential effects of the streptococcal fibronectin binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and Hep-2 tissue culture cells. Infect Immun 64: 2415-2419.
    • (1996) Infect Immun , vol.64 , pp. 2415-2419
    • Courtney, H.S.1    Dale, J.B.2    Hasty, D.L.3
  • 67
    • 0032910564 scopus 로고    scopus 로고
    • Serum opacity factor is a major fibronectin-binding protein and a virulence determinant of M type 2 Streptococcus pyogenes
    • Courtney HS, Hasty DL, Li Y, Chiang HC, Thacker JL & Dale JB (1999) Serum opacity factor is a major fibronectin-binding protein and a virulence determinant of M type 2 Streptococcus pyogenes. Mol Microbiol 32: 89-98.
    • (1999) Mol Microbiol , vol.32 , pp. 89-98
    • Courtney, H.S.1    Hasty, D.L.2    Li, Y.3    Chiang, H.C.4    Thacker, J.L.5    Dale, J.B.6
  • 69
    • 25444495988 scopus 로고    scopus 로고
    • Adherence of Pasteurella multocida to fibronectin
    • Dabo SM, Confer AW & Hartson SD (2005) Adherence of Pasteurella multocida to fibronectin. Vet Microbiol 110: 265-275.
    • (2005) Vet Microbiol , vol.110 , pp. 265-275
    • Dabo, S.M.1    Confer, A.W.2    Hartson, S.D.3
  • 71
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 β subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumonia
    • Dallo SF, Kannan TR, Blaylock MW & Baseman JB (2002) Elongation factor Tu and E1 β subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumonia. Mol Microbiol 46: 1041-1051.
    • (2002) Mol Microbiol , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 72
    • 0036180962 scopus 로고    scopus 로고
    • Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2
    • De Greef A, Buys H, Verhaar R, Dijkstra J, Van AL & Smith HE (2002) Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2. Infect Immun 70: 1319-1325.
    • (2002) Infect Immun , vol.70 , pp. 1319-1325
    • De Greef, A.1    Buys, H.2    Verhaar, R.3    Dijkstra, J.4    Van, A.L.5    Smith, H.E.6
  • 73
    • 34548048636 scopus 로고    scopus 로고
    • Clinical trial of safety and efficacy of INH-A21 for the prevention of nosocomial staphylococcal bloodstream infection in premature infants
    • DeJonge M, Burchfield D, Bloom B et al. (2007) Clinical trial of safety and efficacy of INH-A21 for the prevention of nosocomial staphylococcal bloodstream infection in premature infants. J Pediatr 151: 260-265.
    • (2007) J Pediatr , vol.151 , pp. 260-265
    • DeJonge, M.1    Burchfield, D.2    Bloom, B.3
  • 74
    • 54349128596 scopus 로고    scopus 로고
    • Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus
    • Dent A, Bae T, Missiakas DM & Schneewind O (2008) Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus. EMBO J 27: 2656-2668.
    • (2008) EMBO J , vol.27 , pp. 2656-2668
    • Dent, A.1    Bae, T.2    Missiakas, D.M.3    Schneewind, O.4
  • 75
    • 0038493745 scopus 로고
    • Transformation-enhancing activity of gelatin-binding fragments of fibronectin
    • De Petro G, Barlati S, Vartio T & Vaheri A (1981) Transformation-enhancing activity of gelatin-binding fragments of fibronectin. P Natl Acad Sci USA 78: 4965-4969.
    • (1981) P Natl Acad Sci USA , vol.78 , pp. 4965-4969
    • De Petro, G.1    Barlati, S.2    Vartio, T.3    Vaheri, A.4
  • 76
    • 50949116784 scopus 로고    scopus 로고
    • The cartilage chondrolytic mechanism of fibronectin fragments involves MAP kinases
    • Osteoarthritis Cartilage
    • Ding L, Guo D & Homandberg GA (2008) The cartilage chondrolytic mechanism of fibronectin fragments involves MAP kinases: comparison of three fragments and native fibronectin. Osteoarthritis Cartilage 16: 1253-1262.
    • (2008) comparison of three fragments and native fibronectin , vol.16 , pp. 1253-1262
    • Ding, L.1    Guo, D.2    Homandberg, G.A.3
  • 77
    • 70349260481 scopus 로고    scopus 로고
    • Fibronectin fragments mediate matrix metalloproteinase upregulation and cartilage damage through proline rich tyrosine kinase, c-src, NF-kappaB and protein kinase Cdelta
    • Ding L, Guo D & Homandberg GA (2009) Fibronectin fragments mediate matrix metalloproteinase upregulation and cartilage damage through proline rich tyrosine kinase, c-src, NF-kappaB and protein kinase Cdelta. Osteoarthritis Cartilage 17: 1385-1392.
    • (2009) Osteoarthritis Cartilage , vol.17 , pp. 1385-1392
    • Ding, L.1    Guo, D.2    Homandberg, G.A.3
  • 79
    • 21244452786 scopus 로고    scopus 로고
    • Salmonella enterica serotype Typhimurium MisL is an intestinal colonisation factor that binds fibronectin
    • Dorsey CW, Laarakker MC, Humphries AD, Weening EH & Baumier AJ (2005) Salmonella enterica serotype Typhimurium MisL is an intestinal colonisation factor that binds fibronectin. Mol Microbiol 57: 196-211.
    • (2005) Mol Microbiol , vol.57 , pp. 196-211
    • Dorsey, C.W.1    Laarakker, M.C.2    Humphries, A.D.3    Weening, E.H.4    Baumier, A.J.5
  • 80
    • 0026652432 scopus 로고
    • Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance
    • Downing AK, Driscoll PC, Harvey TS, Dudgeon TJ, Smith BO, Baron M & Campbell ID (1992) Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance. J Mol Biol 225: 821-833.
    • (1992) J Mol Biol , vol.225 , pp. 821-833
    • Downing, A.K.1    Driscoll, P.C.2    Harvey, T.S.3    Dudgeon, T.J.4    Smith, B.O.5    Baron, M.6    Campbell, I.D.7
  • 83
    • 0026079801 scopus 로고
    • Genetic competence in Bacillus subtilis
    • Dubnau D (1991) Genetic competence in Bacillus subtilis. Microbiol Rev 55: 395-424.
    • (1991) Microbiol Rev , vol.55 , pp. 395-424
    • Dubnau, D.1
  • 84
    • 17644380678 scopus 로고    scopus 로고
    • Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405
    • Edwards AM, Jenkinson HF, Woodward MJ & Dymock D (2005) Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405. Infect Immun 73: 2891-2898.
    • (2005) Infect Immun , vol.73 , pp. 2891-2898
    • Edwards, A.M.1    Jenkinson, H.F.2    Woodward, M.J.3    Dymock, D.4
  • 85
    • 35148873213 scopus 로고    scopus 로고
    • Are S-layers exoskeletons? The basic function of protein surface layers revisited
    • Engelhardt H (2007) Are S-layers exoskeletons? The basic function of protein surface layers revisited. J Struct Biol 160: 115-124.
    • (2007) J Struct Biol , vol.160 , pp. 115-124
    • Engelhardt, H.1
  • 87
    • 35048815089 scopus 로고    scopus 로고
    • Host protein binding and adhesive properties of H6 and H7 flagella of attaching and effacing Escherichia coli
    • Erdem AL, Avelino F, Xicohtencatl-Cortes J & Girón JA (2007) Host protein binding and adhesive properties of H6 and H7 flagella of attaching and effacing Escherichia coli. J Bacteriol 189: 7426-7435.
    • (2007) J Bacteriol , vol.189 , pp. 7426-7435
    • Erdem, A.L.1    Avelino, F.2    Xicohtencatl-Cortes, J.3    Girón, J.A.4
  • 88
    • 0021058825 scopus 로고
    • Fibronectin in extended and compact conformations. Electron microscopy and sedimentation analysis
    • Erickson HP & Carrell NA (1983) Fibronectin in extended and compact conformations. Electron microscopy and sedimentation analysis. J Biol Chem 258: 14539-14544.
    • (1983) J Biol Chem , vol.258 , pp. 14539-14544
    • Erickson, H.P.1    Carrell, N.A.2
  • 89
    • 53449101619 scopus 로고    scopus 로고
    • Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis
    • Esgleas M, Li Y, Hancock MA, Harel J, Dubreuil JD & Gottschalk M (2008) Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis. Microbiology 154: 2668-2679.
    • (2008) Microbiology , vol.154 , pp. 2668-2679
    • Esgleas, M.1    Li, Y.2    Hancock, M.A.3    Harel, J.4    Dubreuil, J.D.5    Gottschalk, M.6
  • 90
    • 0043267665 scopus 로고    scopus 로고
    • The Arcanobacterium pyogenes collagen binding protein, CbpA, promotes adhesion to host cells
    • Esmay PA, Billington SJ, Link MA, Songer JG & Jost BH (2003) The Arcanobacterium pyogenes collagen binding protein, CbpA, promotes adhesion to host cells. Infect Immun 71: 4368-4374.
    • (2003) Infect Immun , vol.71 , pp. 4368-4374
    • Esmay, P.A.1    Billington, S.J.2    Link, M.A.3    Songer, J.G.4    Jost, B.H.5
  • 91
    • 0020026495 scopus 로고
    • Isolation of a fibronectin-binding protein from Staphylococcus aureus
    • Espersen F & Clemmensen I (1982) Isolation of a fibronectin-binding protein from Staphylococcus aureus. Infect Immun 37: 526-531.
    • (1982) Infect Immun , vol.37 , pp. 526-531
    • Espersen, F.1    Clemmensen, I.2
  • 93
    • 0004169517 scopus 로고    scopus 로고
    • Leptospira and Leptospirosis
    • 2nd edn. MedSci, Melbourne.
    • Faine S, Adler B, Bolin C & Perolat P (1999) Leptospira and Leptospirosis. 2nd edn. MedSci, Melbourne.
    • (1999)
    • Faine, S.1    Adler, B.2    Bolin, C.3    Perolat, P.4
  • 94
    • 53649099644 scopus 로고    scopus 로고
    • The major pilin subunit of the AAF/II fimbriae from enteroaggregative Escherichia coli mediates binding to the extracellular matrix proteins
    • Farfan MJ, Inman KG & Nataro JP (2008) The major pilin subunit of the AAF/II fimbriae from enteroaggregative Escherichia coli mediates binding to the extracellular matrix proteins. Infect Immun 76: 4378-4384.
    • (2008) Infect Immun , vol.76 , pp. 4378-4384
    • Farfan, M.J.1    Inman, K.G.2    Nataro, J.P.3
  • 95
    • 0031900968 scopus 로고    scopus 로고
    • Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola
    • Fenno JC, Hannam PM, Leung WK, Tamura M, Uitto V-J & McBride BC (1998) Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola. Infect Immun 66: 1869-1877.
    • (1998) Infect Immun , vol.66 , pp. 1869-1877
    • Fenno, J.C.1    Hannam, P.M.2    Leung, W.K.3    Tamura, M.4    Uitto, V.5    McBride, B.C.6
  • 96
    • 0034064780 scopus 로고    scopus 로고
    • Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment
    • Fenno JC, Tamura M, Hannam PM, Wong GWK, Chan RA & McBride BC (2000) Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment. Infect Immun 68: 1884-1892.
    • (2000) Infect Immun , vol.68 , pp. 1884-1892
    • Fenno, J.C.1    Tamura, M.2    Hannam, P.M.3    Wong, G.W.K.4    Chan, R.A.5    McBride, B.C.6
  • 97
    • 0028875886 scopus 로고
    • Alternative splicing of fibronectin - many different proteins but few different functions
    • Ffrench-Constant C (1995) Alternative splicing of fibronectin - many different proteins but few different functions. Exp Cell Res 221: 261-271.
    • (1995) Exp Cell Res , vol.221 , pp. 261-271
    • Ffrench-Constant, C.1
  • 98
    • 0034657179 scopus 로고    scopus 로고
    • Arthropod and host-specific Borrelia burgdorferi bbk32 expression and the inhibition of spirochete transmission
    • Fikrig E, Feng W, Barthold SW, Telford SR & Flavell RA (2000) Arthropod and host-specific Borrelia burgdorferi bbk32 expression and the inhibition of spirochete transmission. J Immunol 164: 5344-5351.
    • (2000) J Immunol , vol.164 , pp. 5344-5351
    • Fikrig, E.1    Feng, W.2    Barthold, S.W.3    Telford, S.R.4    Flavell, R.A.5
  • 99
    • 0036719965 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hap autotransporter binds to fibronectin, laminin and type IV collagen
    • Fink DL, Green BA & St Geme JW (2002) The Haemophilus influenzae Hap autotransporter binds to fibronectin, laminin and type IV collagen. Infect Immun 70: 4902-4907.
    • (2002) Infect Immun , vol.70 , pp. 4902-4907
    • Fink, D.L.1    Green, B.A.2    St Geme, J.W.3
  • 101
    • 29644446929 scopus 로고    scopus 로고
    • Fibronectin binding protein BBK32 of the lyme disease spirochete promotes bacterial attachment to glycosaminoglycans
    • Fischer JR, LeBlanc KT & Leong JM (2006) Fibronectin binding protein BBK32 of the lyme disease spirochete promotes bacterial attachment to glycosaminoglycans. Infect Immun 74: 435-441.
    • (2006) Infect Immun , vol.74 , pp. 435-441
    • Fischer, J.R.1    LeBlanc, K.T.2    Leong, J.M.3
  • 102
    • 55849096919 scopus 로고    scopus 로고
    • Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus
    • Fisher M, Huang YS, Li X, McIver KS, Toukoki C & Eichenbaum Z (2008) Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus. Infect Immun 76: 5006-5015.
    • (2008) Infect Immun , vol.76 , pp. 5006-5015
    • Fisher, M.1    Huang, Y.S.2    Li, X.3    McIver, K.S.4    Toukoki, C.5    Eichenbaum, Z.6
  • 103
    • 33646854563 scopus 로고    scopus 로고
    • The interaction of bacterial pathogens with platelets
    • Fitzgerald JR, Foster TJ & Cox D (2006a) The interaction of bacterial pathogens with platelets. Nature Revs Microbiol 4: 445-457.
    • (2006) Nature Revs Microbiol , vol.4 , pp. 445-457
    • Fitzgerald, J.R.1    Foster, T.J.2    Cox, D.3
  • 104
    • 33645052482 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of Staphylococcus aureus mediate activation of human platelets via fibrinogen and fibronectin bridges to integrin GPIIb/IIIa and IgG binding to the FcgammaRIIa receptor
    • Fitzgerald JR, Loughman A, Keane F, Brennan M, Knobel M, Higgins J, Visai L, Speziale P, Cox D & Foster TJ (2006b) Fibronectin-binding proteins of Staphylococcus aureus mediate activation of human platelets via fibrinogen and fibronectin bridges to integrin GPIIb/IIIa and IgG binding to the FcgammaRIIa receptor. Mol Microbiol 59: 212-230.
    • (2006) Mol Microbiol , vol.59 , pp. 212-230
    • Fitzgerald, J.R.1    Loughman, A.2    Keane, F.3    Brennan, M.4    Knobel, M.5    Higgins, J.6    Visai, L.7    Speziale, P.8    Cox, D.9    Foster, T.J.10
  • 105
    • 66549105468 scopus 로고    scopus 로고
    • Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization
    • Flanagan RC, Neal-McKinney JM, Dhillon AS, Miller WG & Konkel ME (2009) Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization. Infect Immun 77: 2399-2407.
    • (2009) Infect Immun , vol.77 , pp. 2399-2407
    • Flanagan, R.C.1    Neal-McKinney, J.M.2    Dhillon, A.S.3    Miller, W.G.4    Konkel, M.E.5
  • 107
    • 0029936504 scopus 로고    scopus 로고
    • Reconsideration of the role of fibronectin binding in endocarditis caused by Staphylococcus aureus
    • Flock J-I, Hienz SA, Heimdahl A & Schennings T (1996) Reconsideration of the role of fibronectin binding in endocarditis caused by Staphylococcus aureus. Infect Immun 64: 1876-1878.
    • (1996) Infect Immun , vol.64 , pp. 1876-1878
    • Flock, J.1    Hienz, S.A.2    Heimdahl, A.3    Schennings, T.4
  • 108
    • 0033754023 scopus 로고    scopus 로고
    • Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins
    • Fowler T, Wann ER, Joh D, Johansson S, Foster TJ & Hook M (2000) Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins. Eur J Cell Biol 79: 672-679.
    • (2000) Eur J Cell Biol , vol.79 , pp. 672-679
    • Fowler, T.1    Wann, E.R.2    Joh, D.3    Johansson, S.4    Foster, T.J.5    Hook, M.6
  • 109
    • 0038001468 scopus 로고    scopus 로고
    • Src kinase has a central role in in vitro internalisation of Staphylococcus aureus
    • Fowler T, Johansson S, Wary KK & Hook M (2003) Src kinase has a central role in in vitro internalisation of Staphylococcus aureus. Cell Microbiol 5: 417-426.
    • (2003) Cell Microbiol , vol.5 , pp. 417-426
    • Fowler, T.1    Johansson, S.2    Wary, K.K.3    Hook, M.4
  • 110
    • 0029030848 scopus 로고
    • Protein H - bacterial surface proteins with affinity for both immunoglobulin and fibronectin type III domains
    • Frick I-M, Crossin KL, Edelman GM & Bjorck L (1995) Protein H - bacterial surface proteins with affinity for both immunoglobulin and fibronectin type III domains. EMBO J 14: 1674-1679.
    • (1995) EMBO J , vol.14 , pp. 1674-1679
    • Frick, I.1    Crossin, K.L.2    Edelman, G.M.3    Bjorck, L.4
  • 111
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland JC, Lee MH & Boettiger D (2009) Mechanically activated integrin switch controls alpha5beta1 function. Science 323: 642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 112
    • 0021710516 scopus 로고
    • Binding of Escherichia coli to fibronectin. A mechanism of tissue adherence
    • Fröman G, Switalski LM, Faris A, Wadström T & Höök M (1984) Binding of Escherichia coli to fibronectin. A mechanism of tissue adherence. J Biol Chem 259: 14899-14905.
    • (1984) J Biol Chem , vol.259 , pp. 14899-14905
    • Fröman, G.1    Switalski, L.M.2    Faris, A.3    Wadström, T.4    Höök, M.5
  • 113
    • 0344736695 scopus 로고    scopus 로고
    • Structure and functional significance of mechanically unfolded fibronectin type III intermediates
    • Gao M, Craig D, Lequin O, Campbell ID, Vogel V & Schulten K (2003) Structure and functional significance of mechanically unfolded fibronectin type III intermediates. P Natl Acad Sci USA 100: 14784-14789.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 14784-14789
    • Gao, M.1    Craig, D.2    Lequin, O.3    Campbell, I.D.4    Vogel, V.5    Schulten, K.6
  • 114
    • 0028141575 scopus 로고
    • Staphylococcus saprophyticus haemagglutinin binds fibronectin
    • Gatermann S & Meyer H-G (1994) Staphylococcus saprophyticus haemagglutinin binds fibronectin. Infect Immun 62: 4556-4562.
    • (1994) Infect Immun , vol.62 , pp. 4556-4562
    • Gatermann, S.1    Meyer, H.2
  • 115
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George EL, Georges-Labounesse EN, Patel-King RS, Rayburn H & Hynes RO (1993) Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119: 1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labounesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 116
    • 0032702971 scopus 로고    scopus 로고
    • Listeria monocytogenes possesses adhesins for fibronectin
    • Gilot P, Andre P & Content J (1999) Listeria monocytogenes possesses adhesins for fibronectin. Infect Immun 67: 6698-6701.
    • (1999) Infect Immun , vol.67 , pp. 6698-6701
    • Gilot, P.1    Andre, P.2    Content, J.3
  • 117
    • 0033803230 scopus 로고    scopus 로고
    • Cloning, sequencing and characterisation of a Listeria monocytogenes gene encoding a fibronectin-binding protein
    • Gilot P, Jossin Y & Content J (2000) Cloning, sequencing and characterisation of a Listeria monocytogenes gene encoding a fibronectin-binding protein. J Med Microbiol 49: 887-896.
    • (2000) J Med Microbiol , vol.49 , pp. 887-896
    • Gilot, P.1    Jossin, Y.2    Content, J.3
  • 119
    • 0027520723 scopus 로고
    • Adherence of Staphylococcus aureus to cultures of human peritoneal mesothelial cells
    • Glancey G, Cameron JS, Ogg C & Poston S (1993) Adherence of Staphylococcus aureus to cultures of human peritoneal mesothelial cells. Nephrol Dial Transplant 8: 157-162.
    • (1993) Nephrol Dial Transplant , vol.8 , pp. 157-162
    • Glancey, G.1    Cameron, J.S.2    Ogg, C.3    Poston, S.4
  • 120
    • 33749249602 scopus 로고    scopus 로고
    • Identification of OmpU of Vibrio vulnificus as a fibronectin binding protein and its role in bacterial pathogenesis
    • Goo SY, Lee H-J, Kim WH, Han K-L, Park D-K, Lee H-J, Kim SM, Kim K-S, Lee K-H & Park S-J (2006) Identification of OmpU of Vibrio vulnificus as a fibronectin binding protein and its role in bacterial pathogenesis. Infect Immun 74: 5586-5594.
    • (2006) Infect Immun , vol.74 , pp. 5586-5594
    • Goo, S.Y.1    Lee, H.2    Kim, W.H.3    Han, K.4    Park, D.5    Lee, H.6    Kim, S.M.7    Kim, K.8    Lee, K.9    Park, S.10
  • 122
    • 0031822516 scopus 로고    scopus 로고
    • Fibronectin fragments modulate human retinal capillary cell proliferation and migration
    • Grant MB, Caballero S, Bush DM & Spoerri PE (1998) Fibronectin fragments modulate human retinal capillary cell proliferation and migration. Diabetes 47: 1335-1340.
    • (1998) Diabetes , vol.47 , pp. 1335-1340
    • Grant, M.B.1    Caballero, S.2    Bush, D.M.3    Spoerri, P.E.4
  • 124
    • 9244264431 scopus 로고    scopus 로고
    • Truncation of fibronectin-binding proteins in Staphyococcus aureus strain Newman leads to deficient adherence and host cell invasion due to loss of the cell wall anchor function
    • Grundmeier M, Hussain M, Becker P, Heilmann C, Peters G & Sinha B (2004) Truncation of fibronectin-binding proteins in Staphyococcus aureus strain Newman leads to deficient adherence and host cell invasion due to loss of the cell wall anchor function. Infect Immun 72: 7155-7163.
    • (2004) Infect Immun , vol.72 , pp. 7155-7163
    • Grundmeier, M.1    Hussain, M.2    Becker, P.3    Heilmann, C.4    Peters, G.5    Sinha, B.6
  • 125
    • 0032948058 scopus 로고    scopus 로고
    • Protective immune response against Streptococcus pyogenes in mice after intranasal vaccination with fibronectin binding protein Sfb1
    • Guzman CA, Talay SR, Molinari G, Medina E & Chhatwal GS (1999) Protective immune response against Streptococcus pyogenes in mice after intranasal vaccination with fibronectin binding protein Sfb1. J Infect Dis 179: 901-906.
    • (1999) J Infect Dis , vol.179 , pp. 901-906
    • Guzman, C.A.1    Talay, S.R.2    Molinari, G.3    Medina, E.4    Chhatwal, G.S.5
  • 126
    • 4644224116 scopus 로고    scopus 로고
    • The extracellular adherence protein from Staphylococcus aureus inhibits neutrophil binding to endothelial cells
    • Haggar A, Ehrnfelt C, Holgersson J & Flock JI (2004) The extracellular adherence protein from Staphylococcus aureus inhibits neutrophil binding to endothelial cells. Infect Immun 72: 6164-6167.
    • (2004) Infect Immun , vol.72 , pp. 6164-6167
    • Haggar, A.1    Ehrnfelt, C.2    Holgersson, J.3    Flock, J.I.4
  • 127
    • 0026661424 scopus 로고
    • Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes
    • Hanski E & Caparon M (1992) Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes. P Natl Acad Sci USA 89: 6172-6176.
    • (1992) P Natl Acad Sci USA , vol.89 , pp. 6172-6176
    • Hanski, E.1    Caparon, M.2
  • 128
    • 0026469139 scopus 로고
    • Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells
    • Hanski E, Horwitz PA & Caparon MG (1992) Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect Immun 60: 5119-5125.
    • (1992) Infect Immun , vol.60 , pp. 5119-5125
    • Hanski, E.1    Horwitz, P.A.2    Caparon, M.G.3
  • 129
    • 0142074792 scopus 로고    scopus 로고
    • The adhesive and immunomodulating properties of the multifunctional Staphylococcus aureus protein Eap
    • Harraghy N, Hussain M, Haggar A, Chavakis T, Sinha B, Herrmann M & Flock JI (2003) The adhesive and immunomodulating properties of the multifunctional Staphylococcus aureus protein Eap. Microbiology 149: 2701-2707.
    • (2003) Microbiology , vol.149 , pp. 2701-2707
    • Harraghy, N.1    Hussain, M.2    Haggar, A.3    Chavakis, T.4    Sinha, B.5    Herrmann, M.6    Flock, J.I.7
  • 130
    • 0036220868 scopus 로고    scopus 로고
    • The molecular basis of Streptococcus equi infection and disease
    • Harrington DJ, Sutcliffe IC & Chanter N (2002) The molecular basis of Streptococcus equi infection and disease. Microbes Infect 4: 501-510.
    • (2002) Microbes Infect , vol.4 , pp. 501-510
    • Harrington, D.J.1    Sutcliffe, I.C.2    Chanter, N.3
  • 131
    • 0030769052 scopus 로고    scopus 로고
    • The alternatively spliced domains EIIIB and EIIIA of human fibronectin affect cell adhesion and spreading
    • Hashimoto-Uoshima M, Yan YZ, Schneider G & Aukhil I (1997) The alternatively spliced domains EIIIB and EIIIA of human fibronectin affect cell adhesion and spreading. J Cell Sci 110: 2271-2280.
    • (1997) J Cell Sci , vol.110 , pp. 2271-2280
    • Hashimoto-Uoshima, M.1    Yan, Y.Z.2    Schneider, G.3    Aukhil, I.4
  • 133
    • 46249119468 scopus 로고    scopus 로고
    • In LipL32, the major leptospiral lipoprotein, the C terminus is the primary immunogenic domain and mediates interaction with collagen IV and plasma fibronectin
    • Hauk P, Macedo F, Romero EC, Vasconcellos SA, De Morais ZM, Barbosa AS & Ho PL (2008) In LipL32, the major leptospiral lipoprotein, the C terminus is the primary immunogenic domain and mediates interaction with collagen IV and plasma fibronectin. Infect Immun 76: 2642-2650.
    • (2008) Infect Immun , vol.76 , pp. 2642-2650
    • Hauk, P.1    Macedo, F.2    Romero, E.C.3    Vasconcellos, S.A.4    De Morais, Z.M.5    Barbosa, A.S.6    Ho, P.L.7
  • 134
    • 0142042875 scopus 로고    scopus 로고
    • Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis
    • Heilmann C, Thumm G, Chhatwal GS, Hartleib J, Uekötter A & Peters G (2003) Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis. Microbiology 149: 2769-2778.
    • (2003) Microbiology , vol.149 , pp. 2769-2778
    • Heilmann, C.1    Thumm, G.2    Chhatwal, G.S.3    Hartleib, J.4    Uekötter, A.5    Peters, G.6
  • 135
    • 3242702048 scopus 로고    scopus 로고
    • Staphylococcus aureus fibronectin-binding protein (FnBP)-mediated adherence to platelets, and aggregation of platelets induced by FnBPA but not by FnBPB
    • Heilmann C, Niemann S, Sinha B, Herrmann M, Kehrel BE & Peters G (2004) Staphylococcus aureus fibronectin-binding protein (FnBP)-mediated adherence to platelets, and aggregation of platelets induced by FnBPA but not by FnBPB. J Infect Dis 190: 321-329.
    • (2004) J Infect Dis , vol.190 , pp. 321-329
    • Heilmann, C.1    Niemann, S.2    Sinha, B.3    Herrmann, M.4    Kehrel, B.E.5    Peters, G.6
  • 136
    • 21344433812 scopus 로고    scopus 로고
    • The multifunctional Staphylococcus aureus autolysin aaa mediates adherence to immobilized fibrinogen and fibronectin
    • Heilmann C, Hartleib J, Hussain MS & Peters G (2005) The multifunctional Staphylococcus aureus autolysin aaa mediates adherence to immobilized fibrinogen and fibronectin. Infect Immun 73: 4793-4802.
    • (2005) Infect Immun , vol.73 , pp. 4793-4802
    • Heilmann, C.1    Hartleib, J.2    Hussain, M.S.3    Peters, G.4
  • 137
    • 33644766916 scopus 로고    scopus 로고
    • Identification of a domain in Yersinia virulence factor YadA that is crucial for extracellular matrix-specific cell adhesion and uptake
    • Heise T & Dersch P (2006) Identification of a domain in Yersinia virulence factor YadA that is crucial for extracellular matrix-specific cell adhesion and uptake. P Natl Acad Sci USA 103: 3375-3380.
    • (2006) P Natl Acad Sci USA , vol.103 , pp. 3375-3380
    • Heise, T.1    Dersch, P.2
  • 138
    • 0031904826 scopus 로고    scopus 로고
    • Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties
    • Hell W, Meyer HG & Gatermann SG (1998) Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties. Mol Microbiol 29: 871-881.
    • (1998) Mol Microbiol , vol.29 , pp. 871-881
    • Hell, W.1    Meyer, H.G.2    Gatermann, S.G.3
  • 140
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson IR & Nataro JP (2001) Virulence functions of autotransporter proteins. Infect Immun 69: 1231-1243.
    • (2001) Infect Immun , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 141
    • 0034541135 scopus 로고    scopus 로고
    • Autotransporter proteins, evolution and redefining protein secretion
    • Henderson IR, Cappello R & Nataro JP (2000) Autotransporter proteins, evolution and redefining protein secretion. Trends Microbiol 8: 529-532.
    • (2000) Trends Microbiol , vol.8 , pp. 529-532
    • Henderson, I.R.1    Cappello, R.2    Nataro, J.P.3
  • 142
    • 0032246189 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein
    • Hendrixson DR & St.Geme JW (1998) The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein. Mol Cell 2: 841-850.
    • (1998) Mol Cell , vol.2 , pp. 841-850
    • Hendrixson, D.R.1    St.Geme, J.W.2
  • 143
    • 0142011076 scopus 로고    scopus 로고
    • Identification and characterization of a fibronectin-binding protein from Clostridium difficile
    • Hennequin C, Janoir C, Barc M-C, Collignon A & Karjalainen T (2003) Identification and characterization of a fibronectin-binding protein from Clostridium difficile. Microbiology 149: 2779-2787.
    • (2003) Microbiology , vol.149 , pp. 2779-2787
    • Hennequin, C.1    Janoir, C.2    Barc, M.3    Collignon, A.4    Karjalainen, T.5
  • 144
    • 24344483178 scopus 로고    scopus 로고
    • Helicobacter pylori VacA toxin interacts with fibronectin and alters HeLa cell adhesion and cytoskeletal organisation in vitro
    • Hennig EE, Godlewski MM, Butruk E & Ostrowski J (2005) Helicobacter pylori VacA toxin interacts with fibronectin and alters HeLa cell adhesion and cytoskeletal organisation in vitro. FEMS Immunol Med Mic 44: 143-150.
    • (2005) FEMS Immunol Med Mic , vol.44 , pp. 143-150
    • Hennig, E.E.1    Godlewski, M.M.2    Butruk, E.3    Ostrowski, J.4
  • 145
    • 0025284695 scopus 로고
    • The core protein of the matrix-associated heparan sulfate proteoglycan binds to fibronectin
    • Heremans A, De Cock B, Cassiman JJ, Van den Berghe H & David G (1990) The core protein of the matrix-associated heparan sulfate proteoglycan binds to fibronectin. J Biol Chem 265: 8716-8724.
    • (1990) J Biol Chem , vol.265 , pp. 8716-8724
    • Heremans, A.1    De Cock, B.2    Cassiman, J.J.3    Van den Berghe, H.4    David, G.5
  • 146
    • 33749528964 scopus 로고    scopus 로고
    • Phase I dose escalation study to evaluate the safety and pharmacokinetic profile of tefibazumab in subjects with end-stage renal disease requiring hemodialysis
    • Hetherington S, Texter M, Wenzel E, Patti JM, Reynolds L, Shamp T & Swan S (2006) Phase I dose escalation study to evaluate the safety and pharmacokinetic profile of tefibazumab in subjects with end-stage renal disease requiring hemodialysis. Antimicrob Agents Chemother 50: 3499-3500.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 3499-3500
    • Hetherington, S.1    Texter, M.2    Wenzel, E.3    Patti, J.M.4    Reynolds, L.5    Shamp, T.6    Swan, S.7
  • 148
    • 62549115317 scopus 로고    scopus 로고
    • Contribution of (sub)domains of Staphylococcus aureus fibronectin-binding protein to the proinflammatory and procoagulant response of human vascular endothelial cells
    • Heying R, Van De Gevel J, Que YA, Piroth L, Moreillon P & Beekhuizen H (2009) Contribution of (sub)domains of Staphylococcus aureus fibronectin-binding protein to the proinflammatory and procoagulant response of human vascular endothelial cells. Thromb Haemost 101: 495-504.
    • (2009) Thromb Haemost , vol.101 , pp. 495-504
    • Heying, R.1    Van De Gevel, J.2    Que, Y.A.3    Piroth, L.4    Moreillon, P.5    Beekhuizen, H.6
  • 149
    • 70349669108 scopus 로고    scopus 로고
    • Structural analysis of the full-length gene encoding a fibronectin-binding-like protein (CadF) and its adjacent genetic loci within Campylobacter lari
    • Hirayama J, Sekizuka T, Tazumi A, Taneike I, Moore JE, Millar BC & Matsuda M (2009) Structural analysis of the full-length gene encoding a fibronectin-binding-like protein (CadF) and its adjacent genetic loci within Campylobacter lari. BMC Microbiol 9: 192.
    • (2009) BMC Microbiol , vol.9 , pp. 192
    • Hirayama, J.1    Sekizuka, T.2    Tazumi, A.3    Taneike, I.4    Moore, J.E.5    Millar, B.C.6    Matsuda, M.7
  • 150
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk E, Roggenkamp A, Reichenbecher M, Lupas A & Heesemann J (2000) Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J 19: 5989-5999.
    • (2000) EMBO J , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 152
    • 0031057650 scopus 로고    scopus 로고
    • Fibronectin-fragment-induced cartilage chondrolysis is associated with release of catabolic cytokines
    • Homandberg GA, Hui F, Wen C, Purple C, Bewsey K, Koepp H, Huch K & Harris A (1997) Fibronectin-fragment-induced cartilage chondrolysis is associated with release of catabolic cytokines. Biochem J 321: 751-757.
    • (1997) Biochem J , vol.321 , pp. 751-757
    • Homandberg, G.A.1    Hui, F.2    Wen, C.3    Purple, C.4    Bewsey, K.5    Koepp, H.6    Huch, K.7    Harris, A.8
  • 153
    • 22844442206 scopus 로고    scopus 로고
    • Identification and characterization of a novel fibronectin-binding protein gene from Streptococcus equi subspecies zooepidemicus strain VTU211
    • Hong K (2005) Identification and characterization of a novel fibronectin-binding protein gene from Streptococcus equi subspecies zooepidemicus strain VTU211. FEMS Immunol Med Mic 45: 231-237.
    • (2005) FEMS Immunol Med Mic , vol.45 , pp. 231-237
    • Hong, K.1
  • 154
    • 0030761980 scopus 로고    scopus 로고
    • Purification and characterization of human lung fibroblast motility-stimulating factor for human soft tissue sarcoma cells
    • Cancer Res
    • Hu M, Pollock RE & Nicolson GL (1997) Purification and characterization of human lung fibroblast motility-stimulating factor for human soft tissue sarcoma cells: identification as an NH2-terminal fragment of human fibronectin. Cancer Res 57: 3577-3584.
    • (1997) identification as an NH2-terminal fragment of human fibronectin , vol.57 , pp. 3577-3584
    • Hu, M.1    Pollock, R.E.2    Nicolson, G.L.3
  • 157
    • 0035164511 scopus 로고    scopus 로고
    • Identification and characterization of a novel 38.5-kilodalton cell surface protein of Staphylococcus aureus with extended-spectrum binding activity for extracellular matrix and plasma proteins
    • Hussain M, Becker K, Von Eiff EC, Schrenzel J, Peters G & Herrmann M (2001) Identification and characterization of a novel 38.5-kilodalton cell surface protein of Staphylococcus aureus with extended-spectrum binding activity for extracellular matrix and plasma proteins. J Bacteriol 183: 6778-6786.
    • (2001) J Bacteriol , vol.183 , pp. 6778-6786
    • Hussain, M.1    Becker, K.2    Von Eiff, E.C.3    Schrenzel, J.4    Peters, G.5    Herrmann, M.6
  • 159
    • 0345164291 scopus 로고
    • Alteration of cell-surface proteins by viral transformation and proteolysis
    • Hynes RO (1973) Alteration of cell-surface proteins by viral transformation and proteolysis. P Natl Acad Sci USA 70: 3170-3174.
    • (1973) P Natl Acad Sci USA , vol.70 , pp. 3170-3174
    • Hynes, R.O.1
  • 161
    • 0004043397 scopus 로고
    • Fibronectins.
    • Springer-Verlag, New York.
    • Hynes RO (1990) Fibronectins.. Springer-Verlag, New York.
    • (1990)
    • Hynes, R.O.1
  • 163
    • 0036267352 scopus 로고    scopus 로고
    • Identification by flagellum display of an epithelial cell- and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis
    • Hynonen U, Westerlund-Wikstrom B, Palva A & Korhonen TK (2002) Identification by flagellum display of an epithelial cell- and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis. J Bacteriol 184: 3360-3367.
    • (2002) J Bacteriol , vol.184 , pp. 3360-3367
    • Hynonen, U.1    Westerlund-Wikstrom, B.2    Palva, A.3    Korhonen, T.K.4
  • 164
    • 0023906835 scopus 로고
    • Interaction of fibronectin and its gelatin-binding domains with fluorescent-labeled chains of type I collagen
    • Ingham KC, Brew SA & Isaacs BS (1988) Interaction of fibronectin and its gelatin-binding domains with fluorescent-labeled chains of type I collagen. J Biol Chem 263: 4624-4628.
    • (1988) J Biol Chem , vol.263 , pp. 4624-4628
    • Ingham, K.C.1    Brew, S.A.2    Isaacs, B.S.3
  • 165
    • 0028816805 scopus 로고
    • Influence of carbohydrate on structure, stability, and function of gelatin-binding fragments of fibronectin
    • Ingham KC, Brew SA & Novokhatny VV (1995) Influence of carbohydrate on structure, stability, and function of gelatin-binding fragments of fibronectin. Arch Biochem Biophys 316: 235-240.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 235-240
    • Ingham, K.C.1    Brew, S.A.2    Novokhatny, V.V.3
  • 166
    • 0036431513 scopus 로고    scopus 로고
    • Type I collagen contains at least 14 cryptic fibronectin binding sites of similar affinity
    • Ingham KC, Brew SA & Migliorini M (2002) Type I collagen contains at least 14 cryptic fibronectin binding sites of similar affinity. Arch Biochem Biophys 407: 217-223.
    • (2002) Arch Biochem Biophys , vol.407 , pp. 217-223
    • Ingham, K.C.1    Brew, S.A.2    Migliorini, M.3
  • 167
    • 0031871348 scopus 로고    scopus 로고
    • Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells
    • Jadoun J, Ozeri V, Burstein E, Skutelsky E, Hanski E & Sela S (1998) Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells. J Infect Dis 178: 147-158.
    • (1998) J Infect Dis , vol.178 , pp. 147-158
    • Jadoun, J.1    Ozeri, V.2    Burstein, E.3    Skutelsky, E.4    Hanski, E.5    Sela, S.6
  • 168
    • 0029744998 scopus 로고    scopus 로고
    • Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains
    • Jaffe J, Natanson-Yaron S, Caparon MG & Hanski E (1996) Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains. Mol Microbiol 21: 373-384.
    • (1996) Mol Microbiol , vol.21 , pp. 373-384
    • Jaffe, J.1    Natanson-Yaron, S.2    Caparon, M.G.3    Hanski, E.4
  • 169
    • 0037315055 scopus 로고    scopus 로고
    • Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX
    • Jeng A, Sakota V, Li Z, Datta V, Beall B & Nizet V (2003) Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX. J Bacteriol 185: 1208-1217.
    • (2003) J Bacteriol , vol.185 , pp. 1208-1217
    • Jeng, A.1    Sakota, V.2    Li, Z.3    Datta, V.4    Beall, B.5    Nizet, V.6
  • 173
    • 0033016468 scopus 로고    scopus 로고
    • The compact conformation of fibronectin is determined by intramolecular ionic interactions
    • Johnson KJ, Sage H, Briscoe G & Erickson HP (1999) The compact conformation of fibronectin is determined by intramolecular ionic interactions. J Biol Chem 274: 15473-15479.
    • (1999) J Biol Chem , vol.274 , pp. 15473-15479
    • Johnson, K.J.1    Sage, H.2    Briscoe, G.3    Erickson, H.P.4
  • 174
    • 42149139568 scopus 로고    scopus 로고
    • Iron-regulated biofilm formation in Staphylococcus aureus Newman requires ica and the secreted protein Emp
    • Johnson M, Cockayne A & Morrissey JA (2008) Iron-regulated biofilm formation in Staphylococcus aureus Newman requires ica and the secreted protein Emp. Infect Immun 76: 1756-1765.
    • (2008) Infect Immun , vol.76 , pp. 1756-1765
    • Johnson, M.1    Cockayne, A.2    Morrissey, J.A.3
  • 175
    • 0026334144 scopus 로고
    • Two different genes encode fibronectin binding proteins in Staphylococcus aureus. The complete nucleotide sequence and characterization of the second gene
    • Jonsson K, Signas C, Muller HP & Lindberg M (1991) Two different genes encode fibronectin binding proteins in Staphylococcus aureus. The complete nucleotide sequence and characterization of the second gene. Eur J Biochem 202: 1041-1048.
    • (1991) Eur J Biochem , vol.202 , pp. 1041-1048
    • Jonsson, K.1    Signas, C.2    Muller, H.P.3    Lindberg, M.4
  • 176
    • 48249107445 scopus 로고    scopus 로고
    • Fibrinogen binding sites P336 and Y338 of clumping factor A are crucial for Staphylococcus aureus virulence
    • Josefsson E, Higgins J, Foster TJ & Tarkowski A (2008) Fibrinogen binding sites P336 and Y338 of clumping factor A are crucial for Staphylococcus aureus virulence. PLoS ONE 3: e2206.
    • (2008) PLoS ONE , vol.3
    • Josefsson, E.1    Higgins, J.2    Foster, T.J.3    Tarkowski, A.4
  • 179
    • 0027086856 scopus 로고
    • Role of fibronectin in the adherence of Staphylococcus aureus to dermal tissues
    • Kanzaki H & Arata J (1992) Role of fibronectin in the adherence of Staphylococcus aureus to dermal tissues. J Dermatol Sci 4: 87-94.
    • (1992) J Dermatol Sci , vol.4 , pp. 87-94
    • Kanzaki, H.1    Arata, J.2
  • 180
    • 67651021458 scopus 로고    scopus 로고
    • Characterization of two putative fibronectin-binding proteins of Clostridium perfringens
    • Katayama S, Nozu N, Okuda M, Hirota S, Yamasaki T & Hitsumoto Y (2009) Characterization of two putative fibronectin-binding proteins of Clostridium perfringens. Anaerobe 15: 155-159.
    • (2009) Anaerobe , vol.15 , pp. 155-159
    • Katayama, S.1    Nozu, N.2    Okuda, M.3    Hirota, S.4    Yamasaki, T.5    Hitsumoto, Y.6
  • 183
    • 0035142610 scopus 로고    scopus 로고
    • Systemic and mucosal immunizations with fibronectin-binding protein FBP54 induce protective immune responses against Streptococcus pyogenes challenge in mice
    • Kawabata S, Kunitomo E, Terao Y, Nakagawa I, Kikuchi K, Totsuka K & Hamada S (2001) Systemic and mucosal immunizations with fibronectin-binding protein FBP54 induce protective immune responses against Streptococcus pyogenes challenge in mice. Infect Immun 69: 924-930.
    • (2001) Infect Immun , vol.69 , pp. 924-930
    • Kawabata, S.1    Kunitomo, E.2    Terao, Y.3    Nakagawa, I.4    Kikuchi, K.5    Totsuka, K.6    Hamada, S.7
  • 184
    • 33846205499 scopus 로고    scopus 로고
    • Fibrinogen and elastin bind to the same region within the A domain of fibronectin binding protein A, an MSCRAMM of Staphylococcus aureus
    • Keane FM, Loughman A, Valtulina V, Brennan M, Speziale P & Foster TJ (2007) Fibrinogen and elastin bind to the same region within the A domain of fibronectin binding protein A, an MSCRAMM of Staphylococcus aureus. Mol Microbiol 63: 711-723.
    • (2007) Mol Microbiol , vol.63 , pp. 711-723
    • Keane, F.M.1    Loughman, A.2    Valtulina, V.3    Brennan, M.4    Speziale, P.5    Foster, T.J.6
  • 187
    • 4744357952 scopus 로고    scopus 로고
    • BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding
    • Kim JH, Singvall J, Schwarz-Linek U, Johnson BJB, Potts JR & Hok M (2004) BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. J Biol Chem 279: 41706-41714.
    • (2004) J Biol Chem , vol.279 , pp. 41706-41714
    • Kim, J.H.1    Singvall, J.2    Schwarz-Linek, U.3    Johnson, B.J.B.4    Potts, J.R.5    Hok, M.6
  • 188
    • 0345094966 scopus 로고    scopus 로고
    • Fibronectin fragment promotes osteoblast-associated gene expression and biological activity of human osteoblast-like cell
    • Kim TI, Jang JH, Chung CP & Ku Y (2003) Fibronectin fragment promotes osteoblast-associated gene expression and biological activity of human osteoblast-like cell. Biotechnol Lett 25: 2007-2011.
    • (2003) Biotechnol Lett , vol.25 , pp. 2007-2011
    • Kim, T.I.1    Jang, J.H.2    Chung, C.P.3    Ku, Y.4
  • 189
    • 0034114755 scopus 로고    scopus 로고
    • The shdA gene is restricted to serotypes of Salmonella enterica subspecies I and contributes to efficient and prolonged fecal shedding
    • Kingsley RA, Van Amsterdam K, Kramer N & Baumier AJ (2000) The shdA gene is restricted to serotypes of Salmonella enterica subspecies I and contributes to efficient and prolonged fecal shedding. Infect Immun 68: 2720-2727.
    • (2000) Infect Immun , vol.68 , pp. 2720-2727
    • Kingsley, R.A.1    Van Amsterdam, K.2    Kramer, N.3    Baumier, A.J.4
  • 190
    • 0036224264 scopus 로고    scopus 로고
    • Salmonella enterica serotype Typhimurium ShdA is an outer membrane fibronectin binding protein that is expressed in the intestine
    • Kingsley RA, Santos RL, Keestra AM, Adams LG & Baumler AJ (2002) Salmonella enterica serotype Typhimurium ShdA is an outer membrane fibronectin binding protein that is expressed in the intestine. Mol Microbiol 43: 895-905.
    • (2002) Mol Microbiol , vol.43 , pp. 895-905
    • Kingsley, R.A.1    Santos, R.L.2    Keestra, A.M.3    Adams, L.G.4    Baumler, A.J.5
  • 191
    • 3242773717 scopus 로고    scopus 로고
    • Fibronectin binding to the Salmonella enterica serotype Typhimurium ShdA autoransporter protein is inhibited by a monoclonal antibody recognising the A3 repeat
    • Kingsley RA, Abi Ghanem D, Puebla-Osorio N, Keestra AM, Berghman L & Baumier AJ (2004a) Fibronectin binding to the Salmonella enterica serotype Typhimurium ShdA autoransporter protein is inhibited by a monoclonal antibody recognising the A3 repeat. J Bacteriol 186: 4931-4939.
    • (2004) J Bacteriol , vol.186 , pp. 4931-4939
    • Kingsley, R.A.1    Abi Ghanem, D.2    Puebla-Osorio, N.3    Keestra, A.M.4    Berghman, L.5    Baumier, A.J.6
  • 195
    • 0030798150 scopus 로고    scopus 로고
    • Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni
    • Konkel ME, Garvis SG, Tipton S, Anderson DE & Cieplak W (1997) Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni. Mol Microbiol 24: 953-963.
    • (1997) Mol Microbiol , vol.24 , pp. 953-963
    • Konkel, M.E.1    Garvis, S.G.2    Tipton, S.3    Anderson, D.E.4    Cieplak, W.5
  • 196
    • 0033066447 scopus 로고    scopus 로고
    • Identification of the enteropathogens Campylobacter jejuni and Campylobacter coli based on the cadF virulence gene and its product
    • Konkel ME, Gray SA, Kim B, Garvis SG & Yoon J (1999) Identification of the enteropathogens Campylobacter jejuni and Campylobacter coli based on the cadF virulence gene and its product. J Clin Microbiol 37: 510-517.
    • (1999) J Clin Microbiol , vol.37 , pp. 510-517
    • Konkel, M.E.1    Gray, S.A.2    Kim, B.3    Garvis, S.G.4    Yoon, J.5
  • 198
    • 73849129236 scopus 로고    scopus 로고
    • Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence
    • Konkel ME, Larson CL & Flanagan RC (2010) Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence. J Bacteriol 192: 68-76.
    • (2010) J Bacteriol , vol.192 , pp. 68-76
    • Konkel, M.E.1    Larson, C.L.2    Flanagan, R.C.3
  • 199
    • 4644274735 scopus 로고    scopus 로고
    • Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain
    • Kostakioti M & Stathopoulos C (2004) Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain. Infect Immun 72: 5548-5554.
    • (2004) Infect Immun , vol.72 , pp. 5548-5554
    • Kostakioti, M.1    Stathopoulos, C.2
  • 201
    • 0029130366 scopus 로고
    • Characterization of a novel fibronectin-binding surface protein in group A streptococci
    • Kreikemeyer B, Talay SR & Chhatwal GS (1995) Characterization of a novel fibronectin-binding surface protein in group A streptococci. Mol Microbiol 17: 137-145.
    • (1995) Mol Microbiol , vol.17 , pp. 137-145
    • Kreikemeyer, B.1    Talay, S.R.2    Chhatwal, G.S.3
  • 204
    • 48349124615 scopus 로고    scopus 로고
    • Staphylococcus aureus giant protein Ebh is involved in tolerance to transient hyperosmotic pressure
    • Kuroda M, Tanaka Y, Aoki R, Shu D, Tsumoto K & Ohta T (2008) Staphylococcus aureus giant protein Ebh is involved in tolerance to transient hyperosmotic pressure. Biochem Biophys Res Commun 374: 237-241.
    • (2008) Biochem Biophys Res Commun , vol.374 , pp. 237-241
    • Kuroda, M.1    Tanaka, Y.2    Aoki, R.3    Shu, D.4    Tsumoto, K.5    Ohta, T.6
  • 205
    • 0018128410 scopus 로고
    • Fibronectin binds to Staphylococcus aureus
    • Kuusela P (1978) Fibronectin binds to Staphylococcus aureus. Nature 276: 718-720.
    • (1978) Nature , vol.276 , pp. 718-720
    • Kuusela, P.1
  • 206
    • 0024357241 scopus 로고
    • Reduced adherence to traumatised rat heart valves by a low fibronectin-binding mutant of Staphylococcus aureus
    • Kuypers JM & Proctor RA (1989) Reduced adherence to traumatised rat heart valves by a low fibronectin-binding mutant of Staphylococcus aureus. Infect Immun 57: 2306-2312.
    • (1989) Infect Immun , vol.57 , pp. 2306-2312
    • Kuypers, J.M.1    Proctor, R.A.2
  • 207
    • 0025875664 scopus 로고
    • Blood-borne fragments of fibronectin after thermal injury
    • La Celle P, Blumenstock FA & Saba TM (1991) Blood-borne fragments of fibronectin after thermal injury. Blood 77: 2037-2041.
    • (1991) Blood , vol.77 , pp. 2037-2041
    • La Celle, P.1    Blumenstock, F.A.2    Saba, T.M.3
  • 208
    • 0032832395 scopus 로고    scopus 로고
    • The fibronectin binding proteins of Staphylococcus aureus are required for adhesion to and invasion of bovine mammary gland cells
    • Lammers A, Nuijten PJ & Smith HE (1999) The fibronectin binding proteins of Staphylococcus aureus are required for adhesion to and invasion of bovine mammary gland cells. FEMS Microbiol Lett 180: 103-109.
    • (1999) FEMS Microbiol Lett , vol.180 , pp. 103-109
    • Lammers, A.1    Nuijten, P.J.2    Smith, H.E.3
  • 210
    • 0028046519 scopus 로고
    • Group A streptococci efficiently invade human respiratory epithelial cells
    • LaPenta D, Rubens C, Chi E & Cleary PP (1994) Group A streptococci efficiently invade human respiratory epithelial cells. P Natl Acad Sci USA 91: 12115-12119.
    • (1994) P Natl Acad Sci USA , vol.91 , pp. 12115-12119
    • LaPenta, D.1    Rubens, C.2    Chi, E.3    Cleary, P.P.4
  • 213
    • 0030050396 scopus 로고    scopus 로고
    • 2.0A crystal structure of a four domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I & Erickson HP (1996) 2.0A crystal structure of a four domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84: 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 214
    • 42149143704 scopus 로고    scopus 로고
    • Outer membrane protein DsrA is the major fibronectin-binding determinant of Haemophilus influenza
    • Leduc I, Dimitra White C, Nepluev I, Throm RE, Spinola SM & Elkins C (2008) Outer membrane protein DsrA is the major fibronectin-binding determinant of Haemophilus influenza. Infect Immun 76: 1608-1616.
    • (2008) Infect Immun , vol.76 , pp. 1608-1616
    • Leduc, I.1    Dimitra White, C.2    Nepluev, I.3    Throm, R.E.4    Spinola, S.M.5    Elkins, C.6
  • 215
    • 60549098245 scopus 로고    scopus 로고
    • Localisation of the domains of Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin
    • Leduc I, Olsen B & Elkins C (2009) Localisation of the domains of Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin. Infect Immun 77: 657-666.
    • (2009) Infect Immun , vol.77 , pp. 657-666
    • Leduc, I.1    Olsen, B.2    Elkins, C.3
  • 216
    • 67650084629 scopus 로고    scopus 로고
    • Mycobacterium avium subsp. paratuberculosis fibronectin attachment protein activates dendritic cells and induces a Th1 polarization
    • Lee JS, Shin SJ, Collins MT, Jung ID, Jeong YI, Lee CM, Shin YK, Kim D & Park YM (2009) Mycobacterium avium subsp. paratuberculosis fibronectin attachment protein activates dendritic cells and induces a Th1 polarization. Infect Immun 77: 2979-2988.
    • (2009) Infect Immun , vol.77 , pp. 2979-2988
    • Lee, J.S.1    Shin, S.J.2    Collins, M.T.3    Jung, I.D.4    Jeong, Y.I.5    Lee, C.M.6    Shin, Y.K.7    Kim, D.8    Park, Y.M.9
  • 217
  • 218
    • 0033966686 scopus 로고    scopus 로고
    • Chancroid from clinical practice to basic science
    • Lewis DA (2000) Chancroid from clinical practice to basic science. AIDS Patient Care STDS 14: 19-36.
    • (2000) AIDS Patient Care STDS , vol.14 , pp. 19-36
    • Lewis, D.A.1
  • 219
    • 33646950247 scopus 로고    scopus 로고
    • Borrelia burgdorferi lacking BBK32, a fibronectin-binding protein, retains full pathogenicity
    • Li X, Liu X, Beck DS, Kantor FS & Fikrig E (2006) Borrelia burgdorferi lacking BBK32, a fibronectin-binding protein, retains full pathogenicity. Infect Immun 74: 3305-3313.
    • (2006) Infect Immun , vol.74 , pp. 3305-3313
    • Li, X.1    Liu, X.2    Beck, D.S.3    Kantor, F.S.4    Fikrig, E.5
  • 220
    • 0037099692 scopus 로고    scopus 로고
    • Molecular adaptation of Borrelia burgdorferi in the murine host
    • Liang FT, Nelson FK & Fikrig E (2002) Molecular adaptation of Borrelia burgdorferi in the murine host. J Exp Med 196: 275-280.
    • (2002) J Exp Med , vol.196 , pp. 275-280
    • Liang, F.T.1    Nelson, F.K.2    Fikrig, E.3
  • 221
    • 29644445323 scopus 로고    scopus 로고
    • A fibronectin-binding protein from Streptococcus equi binds collagen and modulates cell-mediated collagen gel contraction
    • Liden A, Karlstrom A, Lannergard J, Kalamajski S, Guss B, Rubin K & Ryden C (2006) A fibronectin-binding protein from Streptococcus equi binds collagen and modulates cell-mediated collagen gel contraction. Biochem Biophys Res Commun 340: 604-610.
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 604-610
    • Liden, A.1    Karlstrom, A.2    Lannergard, J.3    Kalamajski, S.4    Guss, B.5    Rubin, K.6    Ryden, C.7
  • 222
    • 38349140674 scopus 로고    scopus 로고
    • A secreted collagen- and fibronectin-binding streptococcal protein modulates cell-mediated collagen gel contraction and interstitial fluid pressure
    • Liden A, Van Wieringen WT, Lannergard J, Kassner A, Heinegard D, Reed RK, Guss B & Rubin K (2008) A secreted collagen- and fibronectin-binding streptococcal protein modulates cell-mediated collagen gel contraction and interstitial fluid pressure. J Biol Chem 283: 1234-1242.
    • (2008) J Biol Chem , vol.283 , pp. 1234-1242
    • Liden, A.1    Van Wieringen, W.T.2    Lannergard, J.3    Kassner, A.4    Heinegard, D.5    Reed, R.K.6    Guss, B.7    Rubin, K.8
  • 223
    • 34548224154 scopus 로고    scopus 로고
    • A domain of the Leptospira LigB contributes to high affinity binding of fibronectin
    • Lin Y-P & Chang Y-F (2007) A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Biochem Biophys Res Commun 362: 443-448.
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 443-448
    • Lin, Y.1    Chang, Y.2
  • 224
    • 54449094484 scopus 로고    scopus 로고
    • Calcium binds to leptospiral immunoglobulin-like protein, LigB, and modulates fibronectin binding
    • Lin Y-P, Raman R, Sharma Y & Chang Y-F (2008) Calcium binds to leptospiral immunoglobulin-like protein, LigB, and modulates fibronectin binding. J Biol Chem 283: 25140-25149.
    • (2008) J Biol Chem , vol.283 , pp. 25140-25149
    • Lin, Y.1    Raman, R.2    Sharma, Y.3    Chang, Y.4
  • 225
    • 69949134804 scopus 로고    scopus 로고
    • Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B
    • Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP & Chang YF (2009a) Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. J Biol Chem 284: 23547-23557.
    • (2009) J Biol Chem , vol.284 , pp. 23547-23557
    • Lin, Y.P.1    Greenwood, A.2    Nicholson, L.K.3    Sharma, Y.4    McDonough, S.P.5    Chang, Y.F.6
  • 226
    • 70349152999 scopus 로고    scopus 로고
    • A novel fibronectin type III module binding motif identified on C-terminus of Leptospira immunoglobulin-like protein, LigB
    • Lin YP, Greenwood A, Yan W, Nicholson LK, Sharma Y, McDonough SP & Chang YF (2009b) A novel fibronectin type III module binding motif identified on C-terminus of Leptospira immunoglobulin-like protein, LigB. Biochem Bioph Res Co 389: 57-62.
    • (2009) Biochem Bioph Res Co , vol.389 , pp. 57-62
    • Lin, Y.P.1    Greenwood, A.2    Yan, W.3    Nicholson, L.K.4    Sharma, Y.5    McDonough, S.P.6    Chang, Y.F.7
  • 227
    • 0025374501 scopus 로고
    • Adhesive proteins of haemagglutinating Staphylococcus aureus isolated from bovine mastitis
    • Lindahl M, Holmberg O & Jonsson P (1990) Adhesive proteins of haemagglutinating Staphylococcus aureus isolated from bovine mastitis. J Gen Microbiol 136: 935-939.
    • (1990) J Gen Microbiol , vol.136 , pp. 935-939
    • Lindahl, M.1    Holmberg, O.2    Jonsson, P.3
  • 229
    • 0027280396 scopus 로고
    • Two different genes coding for fibronectin-binding proteins from Streptococcus dysgalactiae. The complete nucleotide sequences and characterization of the binding domains
    • Lindgren PE, McGavin MJ, Signas C, Guss B, Gurusiddappa S, Hook M & Lindberg M (1993) Two different genes coding for fibronectin-binding proteins from Streptococcus dysgalactiae. The complete nucleotide sequences and characterization of the binding domains. Eur J Biochem 214: 819-827.
    • (1993) Eur J Biochem , vol.214 , pp. 819-827
    • Lindgren, P.E.1    McGavin, M.J.2    Signas, C.3    Guss, B.4    Gurusiddappa, S.5    Hook, M.6    Lindberg, M.7
  • 230
    • 0032900509 scopus 로고    scopus 로고
    • SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibits the binding between fibronectin and collagen
    • Lindmark H & Guss B (1999) SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibits the binding between fibronectin and collagen. Infect Immun 67: 2383-2388.
    • (1999) Infect Immun , vol.67 , pp. 2383-2388
    • Lindmark, H.1    Guss, B.2
  • 231
    • 0029825892 scopus 로고    scopus 로고
    • Fibronectin-binding protein of Streptococcus equi subsp. zooepidemicus
    • Lindmark H, Jacobsson K, Frykberg L & Guss B (1996) Fibronectin-binding protein of Streptococcus equi subsp. zooepidemicus. Infect Immun 64: 3993-3999.
    • (1996) Infect Immun , vol.64 , pp. 3993-3999
    • Lindmark, H.1    Jacobsson, K.2    Frykberg, L.3    Guss, B.4
  • 232
    • 0035055230 scopus 로고    scopus 로고
    • Comparison of the fibronectin-binding protein FNE from Streptococcus equi subspecies equi with FNZ from S. equi subspecies zooepidemicus reveals a major and conserved difference
    • Lindmark H, Nilsson M & Guss B (2001) Comparison of the fibronectin-binding protein FNE from Streptococcus equi subspecies equi with FNZ from S. equi subspecies zooepidemicus reveals a major and conserved difference. Infect Immun 69: 3159-3163.
    • (2001) Infect Immun , vol.69 , pp. 3159-3163
    • Lindmark, H.1    Nilsson, M.2    Guss, B.3
  • 233
    • 0027943212 scopus 로고
    • Tracing the spread of fibronectin type III domains in bacterial glycohydrolases
    • Little E, Bork P & Doolittle RF (1994) Tracing the spread of fibronectin type III domains in bacterial glycohydrolases. J Mol Evol 39: 631-643.
    • (1994) J Mol Evol , vol.39 , pp. 631-643
    • Little, E.1    Bork, P.2    Doolittle, R.F.3
  • 239
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell mediated matrix assembly process
    • Mao Y & Schwarzbauer JE (2005) Fibronectin fibrillogenesis, a cell mediated matrix assembly process. Matrix Biol 24: 389-399.
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 241
    • 0035213652 scopus 로고    scopus 로고
    • Fibronectin-binding protein A of Staphylococcus aureus has multiple, substituting, binding regions that mediate adherence to fibronectin and invasion of endothelial cells
    • Massey RC, Kantzanou MN, Fowler T, Day NP, Schofield K, Wann ER, Berendt AR, Hook M & Peacock SJ (2001) Fibronectin-binding protein A of Staphylococcus aureus has multiple, substituting, binding regions that mediate adherence to fibronectin and invasion of endothelial cells. Cell Microbiol 3: 839-851.
    • (2001) Cell Microbiol , vol.3 , pp. 839-851
    • Massey, R.C.1    Kantzanou, M.N.2    Fowler, T.3    Day, N.P.4    Schofield, K.5    Wann, E.R.6    Berendt, A.R.7    Hook, M.8    Peacock, S.J.9
  • 242
    • 0021020251 scopus 로고
    • Distribution and chemical characterization of regular arrays in the cell wall of strains of the genus Lactobacillus
    • Masuda K & Kawata T (1983) Distribution and chemical characterization of regular arrays in the cell wall of strains of the genus Lactobacillus. FEMS Microbiol Lett 20: 145-150.
    • (1983) FEMS Microbiol Lett , vol.20 , pp. 145-150
    • Masuda, K.1    Kawata, T.2
  • 243
    • 10744230722 scopus 로고    scopus 로고
    • Pathogenic Leptospira species express surface-exposed proteins belonging to the bacterial immunoglobulin superfamily
    • Matsunaga J, Barocchi MA, Croda J et al. (2003) Pathogenic Leptospira species express surface-exposed proteins belonging to the bacterial immunoglobulin superfamily. Mol Microbiol 49: 929-945.
    • (2003) Mol Microbiol , vol.49 , pp. 929-945
    • Matsunaga, J.1    Barocchi, M.A.2    Croda, J.3
  • 244
    • 33644767983 scopus 로고    scopus 로고
    • Identification of fibronectin-binding proteins in Mycoplasma gallisepticum strain R
    • May M, Papazisi L, Gorton TS & Geary SJ (2006) Identification of fibronectin-binding proteins in Mycoplasma gallisepticum strain R. Infect Immun 74: 1777-1785.
    • (2006) Infect Immun , vol.74 , pp. 1777-1785
    • May, M.1    Papazisi, L.2    Gorton, T.S.3    Geary, S.J.4
  • 245
    • 0019200629 scopus 로고
    • Degradation of fibronectin by human leukocyte elastase. Release of biologically active fragments
    • McDonald JA & Kelley DG (1980) Degradation of fibronectin by human leukocyte elastase. Release of biologically active fragments. J Biol Chem 255: 8848-8858.
    • (1980) J Biol Chem , vol.255 , pp. 8848-8858
    • McDonald, J.A.1    Kelley, D.G.2
  • 246
    • 0023178166 scopus 로고
    • Fibronectin's cell adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix
    • McDonald JA, Quade BJ, Broekelmann TJ, LaChance R, Forsman K, Hasegawa E & Akiyama S (1987) Fibronectin's cell adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix. J Biol Chem 262: 2957-2967.
    • (1987) J Biol Chem , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    LaChance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 247
    • 0036084386 scopus 로고    scopus 로고
    • Increased virulence of a fibronectin-binding protein mutant of Staphylococcus aureus in a rat model of pneumonia
    • McElroy MC, Cain DJ, Tyrrell C, Foster TJ & Haslett C (2002) Increased virulence of a fibronectin-binding protein mutant of Staphylococcus aureus in a rat model of pneumonia. Infect Immun 70: 3865-3873.
    • (2002) Infect Immun , vol.70 , pp. 3865-3873
    • McElroy, M.C.1    Cain, D.J.2    Tyrrell, C.3    Foster, T.J.4    Haslett, C.5
  • 248
    • 0031004994 scopus 로고    scopus 로고
    • Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease
    • McGavin MJ, Zahradka C, Rice K & Scott JE (1997) Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease. Infect Immun 65: 2621-2628.
    • (1997) Infect Immun , vol.65 , pp. 2621-2628
    • McGavin, M.J.1    Zahradka, C.2    Rice, K.3    Scott, J.E.4
  • 250
    • 0026728196 scopus 로고
    • Gene disruption identifies a 290 kDa cell-surface polypeptide conferring hydrophobicity and coaggregation properties in Streptococcus gordonii
    • McNab R & Jenkinson HF (1992) Gene disruption identifies a 290 kDa cell-surface polypeptide conferring hydrophobicity and coaggregation properties in Streptococcus gordonii. Mol Microbiol 6: 2939-2949.
    • (1992) Mol Microbiol , vol.6 , pp. 2939-2949
    • McNab, R.1    Jenkinson, H.F.2
  • 251
    • 0028149676 scopus 로고
    • Cell-surface-associated polypeptides CshA and CshB of high molecular mass are colonization determinants in the oral bacterium Streptococcus gordonii
    • McNab R, Jenkinson HF, Loach DM & Tannock GW (1994) Cell-surface-associated polypeptides CshA and CshB of high molecular mass are colonization determinants in the oral bacterium Streptococcus gordonii. Mol Microbiol 14: 743-754.
    • (1994) Mol Microbiol , vol.14 , pp. 743-754
    • McNab, R.1    Jenkinson, H.F.2    Loach, D.M.3    Tannock, G.W.4
  • 252
    • 0029794139 scopus 로고    scopus 로고
    • Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin
    • McNab R, Holmes AR, Clarke JM, Tannock GW & Jenkinson HF (1996) Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin. Infect Immun 64: 4204-4210.
    • (1996) Infect Immun , vol.64 , pp. 4204-4210
    • McNab, R.1    Holmes, A.R.2    Clarke, J.M.3    Tannock, G.W.4    Jenkinson, H.F.5
  • 254
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenza Hia trimeric autotransporter
    • Meng G, Surana NK, Sg Geme J & Waksman G (2006) Structure of the outer membrane translocator domain of the Haemophilus influenza Hia trimeric autotransporter. EMBO J 25: 2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    Sg Geme, J.3    Waksman, G.4
  • 255
    • 0037945207 scopus 로고    scopus 로고
    • The role of fibronectin binding proteins in the pathogenesis of Staphylococcus aureus infections
    • Menzies BE (2003) The role of fibronectin binding proteins in the pathogenesis of Staphylococcus aureus infections. Curr Opin Infect Dis 16: 225-229.
    • (2003) Curr Opin Infect Dis , vol.16 , pp. 225-229
    • Menzies, B.E.1
  • 256
    • 0036534725 scopus 로고    scopus 로고
    • Inhibition of staphylococcal wound infection and potentiation of antibiotic prophylaxis by a recombinant fragment of the fibronectin-binding protein of Staphylococcus aureus
    • Menzies BE, Kourteva Y, Kaiser AB & Kernodle DS (2002) Inhibition of staphylococcal wound infection and potentiation of antibiotic prophylaxis by a recombinant fragment of the fibronectin-binding protein of Staphylococcus aureus. J Infect Dis 185: 937-943.
    • (2002) J Infect Dis , vol.185 , pp. 937-943
    • Menzies, B.E.1    Kourteva, Y.2    Kaiser, A.B.3    Kernodle, D.S.4
  • 257
    • 0034175911 scopus 로고    scopus 로고
    • Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae
    • Merien F, Truccolo J, Baranton G & Perolat P (2000) Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae. FEMS Microbiol Lett 185: 17-22.
    • (2000) FEMS Microbiol Lett , vol.185 , pp. 17-22
    • Merien, F.1    Truccolo, J.2    Baranton, G.3    Perolat, P.4
  • 259
    • 23644433820 scopus 로고    scopus 로고
    • Gelatin binding to the 8F19F1 module pair of human fibronectin requires site-specific N-glycosylation
    • Millard CJ, Campbell ID & Pickford AR (2005) Gelatin binding to the 8F19F1 module pair of human fibronectin requires site-specific N-glycosylation. FEBS Lett 579: 4529-4534.
    • (2005) FEBS Lett , vol.579 , pp. 4529-4534
    • Millard, C.J.1    Campbell, I.D.2    Pickford, A.R.3
  • 260
    • 44649111167 scopus 로고    scopus 로고
    • Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin
    • Miller-Torbert TA, Sharma S & Holt RG (2008) Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin. Microb Pathog 45: 53-59.
    • (2008) Microb Pathog , vol.45 , pp. 53-59
    • Miller-Torbert, T.A.1    Sharma, S.2    Holt, R.G.3
  • 261
    • 0030903802 scopus 로고    scopus 로고
    • The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells
    • Molinari G, Talay SR, Valentin-Weigand P, Rohde M & Chhatwal GS (1997) The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect Immun 65: 1357-1363.
    • (1997) Infect Immun , vol.65 , pp. 1357-1363
    • Molinari, G.1    Talay, S.R.2    Valentin-Weigand, P.3    Rohde, M.4    Chhatwal, G.S.5
  • 262
    • 0036156141 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of Staphylococcus aureus are involved in adherence to human airway epithelium
    • Mongodin E, Bajolet O, Cutrona J, Bonnet N, Dupuit F, Puchelle E & De Bentzmann S (2002) Fibronectin-binding proteins of Staphylococcus aureus are involved in adherence to human airway epithelium. Infect Immun 70: 620-630.
    • (2002) Infect Immun , vol.70 , pp. 620-630
    • Mongodin, E.1    Bajolet, O.2    Cutrona, J.3    Bonnet, N.4    Dupuit, F.5    Puchelle, E.6    De Bentzmann, S.7
  • 263
    • 0036892861 scopus 로고    scopus 로고
    • Fibronectin-facilitated invasion of T84 eukaryotic cells by Campylobacter jejuni occurs preferentially at the basolateral cell surface
    • Monteville MR & Konkel ME (2002) Fibronectin-facilitated invasion of T84 eukaryotic cells by Campylobacter jejuni occurs preferentially at the basolateral cell surface. Infect Immun 70: 6665-6671.
    • (2002) Infect Immun , vol.70 , pp. 6665-6671
    • Monteville, M.R.1    Konkel, M.E.2
  • 264
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla A, Zhang Z & Ruoslahti E (1994) Superfibronectin is a functionally distinct form of fibronectin. Nature 367: 193-196.
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 266
    • 40749111917 scopus 로고    scopus 로고
    • A novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats
    • Mullen L, Nair SP, Ward JM, Rycroft AN, Williams RA, Robertson G & Henderson B (2008a) A novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats. Infect Immun 76: 1093-1204.
    • (2008) Infect Immun , vol.76 , pp. 1093-1204
    • Mullen, L.1    Nair, S.P.2    Ward, J.M.3    Rycroft, A.N.4    Williams, R.A.5    Robertson, G.6    Henderson, B.7
  • 270
    • 0033841135 scopus 로고    scopus 로고
    • Advances in our understanding of the bone and joint pathology caused by Staphylococcus aureus infection
    • Nair SP, Williams RJ & Henderson B (2000) Advances in our understanding of the bone and joint pathology caused by Staphylococcus aureus infection. Rheumatology 39: 821-834.
    • (2000) Rheumatology , vol.39 , pp. 821-834
    • Nair, S.P.1    Williams, R.J.2    Henderson, B.3
  • 271
    • 0032579246 scopus 로고    scopus 로고
    • The novel fibronectin-binding motif and key residues of mycobacteria
    • Naito M, Ohara N, Matsumoto S & Yamada T (1998) The novel fibronectin-binding motif and key residues of mycobacteria. J Biol Chem 273: 2905-2909.
    • (1998) J Biol Chem , vol.273 , pp. 2905-2909
    • Naito, M.1    Ohara, N.2    Matsumoto, S.3    Yamada, T.4
  • 272
    • 0034194278 scopus 로고    scopus 로고
    • The domains of human fibronectin mediating the binding of α antigen, the most immunopotent antigen of mycobacteria that induces protective immunity against mycobacterial infection
    • Naito M, Fukuda T, Sekiguchi K, Yamada T & Naito M (2000) The domains of human fibronectin mediating the binding of α antigen, the most immunopotent antigen of mycobacteria that induces protective immunity against mycobacterial infection. Biochem J 347: 725-731.
    • (2000) Biochem J , vol.347 , pp. 725-731
    • Naito, M.1    Fukuda, T.2    Sekiguchi, K.3    Yamada, T.4    Naito, M.5
  • 274
    • 0028955430 scopus 로고
    • Distribution of fibronectin-binding proteins among group A streptococci of different M types
    • Natanson S, Sela S, Moses AE, Musser JM, Caparon MG & Hanski E (1995) Distribution of fibronectin-binding proteins among group A streptococci of different M types. J Infect Dis 171: 871-878.
    • (1995) J Infect Dis , vol.171 , pp. 871-878
    • Natanson, S.1    Sela, S.2    Moses, A.E.3    Musser, J.M.4    Caparon, M.G.5    Hanski, E.6
  • 277
    • 0025779466 scopus 로고
    • Fibronectin fragments released from phorbol ester-stimulated pulmonary artery endothelial cell monolayers promote neutrophil chemotaxis
    • Odekon LE, Frewin MB, Del Vecchio P, Saba TM & Gudewicz PW (1991) Fibronectin fragments released from phorbol ester-stimulated pulmonary artery endothelial cell monolayers promote neutrophil chemotaxis. Immunology 74: 114-120.
    • (1991) Immunology , vol.74 , pp. 114-120
    • Odekon, L.E.1    Frewin, M.B.2    Del Vecchio, P.3    Saba, T.M.4    Gudewicz, P.W.5
  • 278
    • 0142130853 scopus 로고    scopus 로고
    • Bacterial Adhesion to Animal Cells and Tissues
    • ASM Press, Washington, DC.
    • Ofek I, Hasty DL & Doyle RJ (2003a) Bacterial Adhesion to Animal Cells and Tissues. ASM Press, Washington, DC.
    • (2003)
    • Ofek, I.1    Hasty, D.L.2    Doyle, R.J.3
  • 279
    • 0142042801 scopus 로고    scopus 로고
    • Anti-adhesion therapy of bacterial diseases
    • FEMS Immunol Med Mic
    • Ofek I, Hasty DL & Sharon N (2003b) Anti-adhesion therapy of bacterial diseases: prospects and problems. FEMS Immunol Med Mic 38: 181-191.
    • (2003) prospects and problems , vol.38 , pp. 181-191
    • Ofek, I.1    Hasty, D.L.2    Sharon, N.3
  • 280
    • 0034948548 scopus 로고    scopus 로고
    • Staphylococcus epdermidis biofilms
    • J Med Microbiol
    • O'Gara JP & Humphreys H (2001) Staphylococcus epdermidis biofilms: importance and implications. J Med Microbiol 50: 582-587.
    • (2001) importance and implications , vol.50 , pp. 582-587
    • O'Gara, J.P.1    Humphreys, H.2
  • 281
    • 0028919003 scopus 로고
    • Characterization of the gene encoding the MPB51, one of the major secreted protein antigens of Mycobacterium bovis BCG, and identification of the secreted protein closely related to the fibronectin binding 85 complex
    • Ohara N, Kitaura H, Hotokezaka H, Nishiyama T, Wada N, Matsumoto S, Matsuo T, Naito M & Yamada T (1995) Characterization of the gene encoding the MPB51, one of the major secreted protein antigens of Mycobacterium bovis BCG, and identification of the secreted protein closely related to the fibronectin binding 85 complex. Scand J Immunol 41: 433-442.
    • (1995) Scand J Immunol , vol.41 , pp. 433-442
    • Ohara, N.1    Kitaura, H.2    Hotokezaka, H.3    Nishiyama, T.4    Wada, N.5    Matsumoto, S.6    Matsuo, T.7    Naito, M.8    Yamada, T.9
  • 282
    • 0033515070 scopus 로고    scopus 로고
    • Dynamics and elasticity of the fibronectin matrix in living cell culture visualised by fibronectin-green fluorescent protein
    • Ohashi T, Kiehart DP & Erickson HP (1999) Dynamics and elasticity of the fibronectin matrix in living cell culture visualised by fibronectin-green fluorescent protein. P Natl Acad Sci USA 96: 2153-2158.
    • (1999) P Natl Acad Sci USA , vol.96 , pp. 2153-2158
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 283
    • 0024498519 scopus 로고
    • Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli
    • Olsén A, Jonsson A & Normark S (1989) Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli. Nature 338: 652-655.
    • (1989) Nature , vol.338 , pp. 652-655
    • Olsén, A.1    Jonsson, A.2    Normark, S.3
  • 284
    • 33645079390 scopus 로고    scopus 로고
    • Molecular basis of fusB-mediated resistance to fusidic acid in Staphylococcus aureus
    • O'Neill AJ & Chopra I (2006) Molecular basis of fusB-mediated resistance to fusidic acid in Staphylococcus aureus. Mol Microbiol 59: 664-676.
    • (2006) Mol Microbiol , vol.59 , pp. 664-676
    • O'Neill, A.J.1    Chopra, I.2
  • 286
    • 20444435483 scopus 로고    scopus 로고
    • Crystal structure of the haemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli
    • Otto BR, Sijbrandi R, Luirink J, Oudega B, Heddle JG, Mitzutani K, Park SY & Tame JR (2005) Crystal structure of the haemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. J Biol Chem 280: 17339-17345.
    • (2005) J Biol Chem , vol.280 , pp. 17339-17345
    • Otto, B.R.1    Sijbrandi, R.2    Luirink, J.3    Oudega, B.4    Heddle, J.G.5    Mitzutani, K.6    Park, S.Y.7    Tame, J.R.8
  • 287
    • 38549160590 scopus 로고    scopus 로고
    • Targeted immunotherapy for staphylococcal infections
    • BioDrugs
    • Otto M (2008) Targeted immunotherapy for staphylococcal infections: focus on anti-MSCRAMM antibodies. BioDrugs 22: 27-36.
    • (2008) focus on anti-MSCRAMM antibodies , vol.22 , pp. 27-36
    • Otto, M.1
  • 289
    • 0031789927 scopus 로고    scopus 로고
    • Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1
    • Ozeri V, Rosenshine I, Mosher DF, Fassler R & Hanski E (1998) Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1. Mol Microbiol 30: 625-637.
    • (1998) Mol Microbiol , vol.30 , pp. 625-637
    • Ozeri, V.1    Rosenshine, I.2    Mosher, D.F.3    Fassler, R.4    Hanski, E.5
  • 290
    • 0034883769 scopus 로고    scopus 로고
    • De novo formation of focal complex-like structures in host cells by invading Streptococci
    • Ozeri V, Rosenshine I, Ben-Ze'Ev A, Bokoch GM, Jou TS & Hanski E (2001) De novo formation of focal complex-like structures in host cells by invading Streptococci. Mol Microbiol 41: 561-573.
    • (2001) Mol Microbiol , vol.41 , pp. 561-573
    • Ozeri, V.1    Rosenshine, I.2    Ben-Ze'Ev, A.3    Bokoch, G.M.4    Jou, T.S.5    Hanski, E.6
  • 291
    • 0036840589 scopus 로고    scopus 로고
    • Cloning and molecular characterization of an immunogenic LigA protein of Leptospira interrogans
    • Palaniappan RU, Chang YF, Jusuf SS et al. (2002) Cloning and molecular characterization of an immunogenic LigA protein of Leptospira interrogans. Infect Immun 70: 5924-5930.
    • (2002) Infect Immun , vol.70 , pp. 5924-5930
    • Palaniappan, R.U.1    Chang, Y.F.2    Jusuf, S.S.3
  • 292
    • 13944272573 scopus 로고    scopus 로고
    • Fibronectin-binding proteins and fibrinogen-binding clumping factors play distinct roles in staphylococcal arthritis and systemic inflammation
    • Palmqvist N, Foster T, Fitzgerald JR, Josefsson E & Tarkowski A (2005) Fibronectin-binding proteins and fibrinogen-binding clumping factors play distinct roles in staphylococcal arthritis and systemic inflammation. J Infect Dis 191: 791-798.
    • (2005) J Infect Dis , vol.191 , pp. 791-798
    • Palmqvist, N.1    Foster, T.2    Fitzgerald, J.R.3    Josefsson, E.4    Tarkowski, A.5
  • 293
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi V & Fischetti VA (1992) A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J Exp Med 176: 415-426.
    • (1992) J Exp Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 294
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R & Yamada KM (2002) Fibronectin at a glance. J Cell Sci 115: 3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 295
    • 0034862585 scopus 로고    scopus 로고
    • In search of the Helicobacter pylori VacA mechanisms
    • Papini E, Zoratti M & Cover TL (2001) In search of the Helicobacter pylori VacA mechanisms. Toxicon 39: 1757-1767.
    • (2001) Toxicon , vol.39 , pp. 1757-1767
    • Papini, E.1    Zoratti, M.2    Cover, T.L.3
  • 296
    • 0023405931 scopus 로고
    • Organisation of the fibronectin gene provides evidence for exon shuffling during evolution
    • Patel RS, Odermatt E, Schwarzbauer JE & Hynes RO (1987) Organisation of the fibronectin gene provides evidence for exon shuffling during evolution. EMBO J 6: 2565-2572.
    • (1987) EMBO J , vol.6 , pp. 2565-2572
    • Patel, R.S.1    Odermatt, E.2    Schwarzbauer, J.E.3    Hynes, R.O.4
  • 297
    • 30644480293 scopus 로고    scopus 로고
    • Vaccines and immunotherapy for staphylococcal infections
    • Patti JM (2005) Vaccines and immunotherapy for staphylococcal infections. Int J Artif Organs 28: 1157-1162.
    • (2005) Int J Artif Organs , vol.28 , pp. 1157-1162
    • Patti, J.M.1
  • 298
  • 299
    • 0033396514 scopus 로고    scopus 로고
    • Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells
    • Peacock SJ, Foster TJ, Cameron BJ & Berendt AR (1999) Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells. Microbiology 145: 3477-3486.
    • (1999) Microbiology , vol.145 , pp. 3477-3486
    • Peacock, S.J.1    Foster, T.J.2    Cameron, B.J.3    Berendt, A.R.4
  • 300
    • 0033836732 scopus 로고    scopus 로고
    • Clinical isolates of Staphylococcus aureus exhibit diversity in fnb genes and adhesion to human fibronectin
    • Peacock SJ, Day NP, Thomas MG, Berendt AR & Foster TJ (2000) Clinical isolates of Staphylococcus aureus exhibit diversity in fnb genes and adhesion to human fibronectin. J Infect 41: 23-31.
    • (2000) J Infect , vol.41 , pp. 23-31
    • Peacock, S.J.1    Day, N.P.2    Thomas, M.G.3    Berendt, A.R.4    Foster, T.J.5
  • 301
    • 0027451948 scopus 로고
    • Mechanism of interaction of the 85B secreted protein of Mycobacterium bovis with fibronectin
    • Peake P, Gooley A & Britton WJ (1993) Mechanism of interaction of the 85B secreted protein of Mycobacterium bovis with fibronectin. Infect Immun 61: 4828-4832.
    • (1993) Infect Immun , vol.61 , pp. 4828-4832
    • Peake, P.1    Gooley, A.2    Britton, W.J.3
  • 302
    • 84906418491 scopus 로고
    • Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins P1 and P2
    • Peterson K, Baseman JB & Alderete JF (1987) Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins P1 and P2. Gentourin Med 63: 355-360.
    • (1987) Gentourin Med , vol.63 , pp. 355-360
    • Peterson, K.1    Baseman, J.B.2    Alderete, J.F.3
  • 303
    • 0020618104 scopus 로고
    • Treponema pallidum receptor binding proteins interact with fibronectin
    • Peterson KM, Baseman JB & Alderete JF (1983) Treponema pallidum receptor binding proteins interact with fibronectin. J Exp Med 157: 1958-1970.
    • (1983) J Exp Med , vol.157 , pp. 1958-1970
    • Peterson, K.M.1    Baseman, J.B.2    Alderete, J.F.3
  • 304
    • 4344566132 scopus 로고    scopus 로고
    • Fibronectin fragments elevate nitric oxide (NO) and inducible NO synthetase (iNOS) levels in bovine cartilage and iNOS inhibitors block fibronectin fragment mediated damage and promote repair
    • Pichika R & Homandberg GA (2004) Fibronectin fragments elevate nitric oxide (NO) and inducible NO synthetase (iNOS) levels in bovine cartilage and iNOS inhibitors block fibronectin fragment mediated damage and promote repair. Inflamm Res 53: 405-412.
    • (2004) Inflamm Res , vol.53 , pp. 405-412
    • Pichika, R.1    Homandberg, G.A.2
  • 305
    • 84941834466 scopus 로고
    • Fibronectin is synthesised as an acute phase reactant in rat hepatocytes
    • Pick-Kober KH, Munker D & Gressner AM (1986) Fibronectin is synthesised as an acute phase reactant in rat hepatocytes. J Clin Chem Clin Biochem 24: 521-528.
    • (1986) J Clin Chem Clin Biochem , vol.24 , pp. 521-528
    • Pick-Kober, K.H.1    Munker, D.2    Gressner, A.M.3
  • 306
    • 0035794672 scopus 로고    scopus 로고
    • The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding
    • Pickford AR, Smith SP, Staunton D, Boyd J & Campbell ID (2001) The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J 20: 1519-1529.
    • (2001) EMBO J , vol.20 , pp. 1519-1529
    • Pickford, A.R.1    Smith, S.P.2    Staunton, D.3    Boyd, J.4    Campbell, I.D.5
  • 307
    • 35448966542 scopus 로고    scopus 로고
    • Functional and structural properties of CbpA, a collagen-binding protein from Arcanobacterium pyogenes
    • Pietrocola G, Valtulina V, Rindi S, Jost BH & Speziale P (2007) Functional and structural properties of CbpA, a collagen-binding protein from Arcanobacterium pyogenes. Microbiology 153: 3380-3389.
    • (2007) Microbiology , vol.153 , pp. 3380-3389
    • Pietrocola, G.1    Valtulina, V.2    Rindi, S.3    Jost, B.H.4    Speziale, P.5
  • 308
    • 48849095070 scopus 로고    scopus 로고
    • The fibrinogen- and fibronectin-binding domains of Staphylococcus aureus fibronectin-binding protein A synergistically promote endothelial invasion and experimental endocarditis
    • Piroth L, Que YA, Widmer E, Panchaud A, Piu S, Entenza JM & Moreillon P (2008) The fibrinogen- and fibronectin-binding domains of Staphylococcus aureus fibronectin-binding protein A synergistically promote endothelial invasion and experimental endocarditis. Infect Immun 76: 3824-3831.
    • (2008) Infect Immun , vol.76 , pp. 3824-3831
    • Piroth, L.1    Que, Y.A.2    Widmer, E.3    Panchaud, A.4    Piu, S.5    Entenza, J.M.6    Moreillon, P.7
  • 310
    • 0030298383 scopus 로고    scopus 로고
    • Structure and function of fibronectin modules
    • Potts JR & Campbell ID (1996) Structure and function of fibronectin modules. Matrix Biology 15: 313-320.
    • (1996) Matrix Biology , vol.15 , pp. 313-320
    • Potts, J.R.1    Campbell, I.D.2
  • 311
  • 313
    • 0031769859 scopus 로고    scopus 로고
    • Identification of a 47kDa fibronectin binding protein expressed by Borrelia burgorferi isolate B31
    • Probert WS & Johnson BJ (1998) Identification of a 47kDa fibronectin binding protein expressed by Borrelia burgorferi isolate B31. Mol Microbiol 30: 1003-1015.
    • (1998) Mol Microbiol , vol.30 , pp. 1003-1015
    • Probert, W.S.1    Johnson, B.J.2
  • 314
    • 0035007253 scopus 로고    scopus 로고
    • Mapping the ligand binding region of Borrelia burgdorferi fibronectin-binding protein BBK32
    • Probert WS, Kim JH, Hook M & Johnson BJB (2001) Mapping the ligand binding region of Borrelia burgdorferi fibronectin-binding protein BBK32. Infect Immun 69: 4129-4135.
    • (2001) Infect Immun , vol.69 , pp. 4129-4135
    • Probert, W.S.1    Kim, J.H.2    Hook, M.3    Johnson, B.J.B.4
  • 315
    • 0032896753 scopus 로고    scopus 로고
    • ComEA is a DNA receptor for transformation of competent Bacillus subtilis
    • Provvedi R & Dubnau D (1999) ComEA is a DNA receptor for transformation of competent Bacillus subtilis. Mol Microbiol 31: 271-280.
    • (1999) Mol Microbiol , vol.31 , pp. 271-280
    • Provvedi, R.1    Dubnau, D.2
  • 316
    • 0034836914 scopus 로고    scopus 로고
    • Reassessing the role of Staphylococcus aureus clumping factor and fibronectin-binding protein by expression in Lactococcuslactis
    • Que YA, François P, Haefliger JA, Entenza JM, Vaudaux P & Moreillon P (2001) Reassessing the role of Staphylococcus aureus clumping factor and fibronectin-binding protein by expression in Lactococcuslactis. Infect Immun 69: 6296-6302.
    • (2001) Infect Immun , vol.69 , pp. 6296-6302
    • Que, Y.A.1    François, P.2    Haefliger, J.A.3    Entenza, J.M.4    Vaudaux, P.5    Moreillon, P.6
  • 317
    • 21144433633 scopus 로고    scopus 로고
    • Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis
    • Que YA, Haefliger JA, Piroth L et al. (2005) Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis. J Exp Med 201: 1627-1635.
    • (2005) J Exp Med , vol.201 , pp. 1627-1635
    • Que, Y.A.1    Haefliger, J.A.2    Piroth, L.3
  • 318
    • 21444441457 scopus 로고    scopus 로고
    • Borrelia burgdorferi binds fibronectin through a tandem β-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci and spirochetes
    • Raibaud S, Schwarz-Linek U, Kim JH, Jenkins HT, Baines ER, Gurusiddappa S, Hook M & Potts JR (2005) Borrelia burgdorferi binds fibronectin through a tandem β-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci and spirochetes. J Biol Chem 250: 18803-18809.
    • (2005) J Biol Chem , vol.250 , pp. 18803-18809
    • Raibaud, S.1    Schwarz-Linek, U.2    Kim, J.H.3    Jenkins, H.T.4    Baines, E.R.5    Gurusiddappa, S.6    Hook, M.7    Potts, J.R.8
  • 320
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin S, Yogev D & Naot Y (1998) Molecular biology and pathogenicity of mycoplasmas. Microbiol Mol Biol Res 62: 1094-1156.
    • (1998) Microbiol Mol Biol Res , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 321
    • 0033396455 scopus 로고    scopus 로고
    • Interactions of the Pseudomonas aeruginosa outer membrane proteins with plasma fibronectins
    • Rebière-Huët J, Di Martino P, Gallet O & Hulen C (1999) Interactions of the Pseudomonas aeruginosa outer membrane proteins with plasma fibronectins. CR Acad Sci III 322: 1071-1080.
    • (1999) CR Acad Sci III , vol.322 , pp. 1071-1080
    • Rebière-Huët, J.1    Di Martino, P.2    Gallet, O.3    Hulen, C.4
  • 323
    • 3442881921 scopus 로고    scopus 로고
    • Inhibition of Pseudomonas aeruginosa adhesion to fibronectin by PA-IL and monosaccharides
    • Can J Microbiol
    • Rebière-Huët J, Di Martino P & Hulen C (2004) Inhibition of Pseudomonas aeruginosa adhesion to fibronectin by PA-IL and monosaccharides: involvement of a lectin-like process. Can J Microbiol 50: 303-312.
    • (2004) involvement of a lectin-like process , vol.50 , pp. 303-312
    • Rebière-Huët, J.1    Di Martino, P.2    Hulen, C.3
  • 324
  • 326
    • 0034678405 scopus 로고    scopus 로고
    • Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis
    • Redick SD, Settles DL, Briscoe G & Erickson HP (2000) Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis. J Cell Biol 149: 521-527.
    • (2000) J Cell Biol , vol.149 , pp. 521-527
    • Redick, S.D.1    Settles, D.L.2    Briscoe, G.3    Erickson, H.P.4
  • 327
    • 0035858128 scopus 로고    scopus 로고
    • Antibodies against a truncated Staphylococcus aureus fibronectin-binding protein protect against dissemination of infection in the rat
    • Rennermalm A, Li YH, Bohaufs L, Jarstrand C, Brauner A, Brennan FR & Flock JI (2001) Antibodies against a truncated Staphylococcus aureus fibronectin-binding protein protect against dissemination of infection in the rat. Vaccine 19: 3376-3383.
    • (2001) Vaccine , vol.19 , pp. 3376-3383
    • Rennermalm, A.1    Li, Y.H.2    Bohaufs, L.3    Jarstrand, C.4    Brauner, A.5    Brennan, F.R.6    Flock, J.I.7
  • 329
    • 9244259664 scopus 로고    scopus 로고
    • Bartonella adhesin A mediates a proangiogenic host cell response
    • Riess T, Andersson SG, Lupas A et al. (2004) Bartonella adhesin A mediates a proangiogenic host cell response. J Exp Med 200: 1267-1278.
    • (2004) J Exp Med , vol.200 , pp. 1267-1278
    • Riess, T.1    Andersson, S.G.2    Lupas, A.3
  • 330
    • 33845985644 scopus 로고    scopus 로고
    • Analysis of Bartonella adhesin A expression revels differences between various B. henselae strains
    • Riess T, Radatz G, Linke D, Schafer A & Kempf VA (2007) Analysis of Bartonella adhesin A expression revels differences between various B. henselae strains. Infect Immun 75: 35-43.
    • (2007) Infect Immun , vol.75 , pp. 35-43
    • Riess, T.1    Radatz, G.2    Linke, D.3    Schafer, A.4    Kempf, V.A.5
  • 332
    • 16644375299 scopus 로고    scopus 로고
    • MSCRAMM-targeted vaccines and immunotherapy for staphylococcal infections
    • Rivas JM, Speziale P, Patti JM & Hook M (2004) MSCRAMM-targeted vaccines and immunotherapy for staphylococcal infections. Curr Opin Drug Discov Devel 7: 223-227.
    • (2004) Curr Opin Drug Discov Devel , vol.7 , pp. 223-227
    • Rivas, J.M.1    Speziale, P.2    Patti, J.M.3    Hook, M.4
  • 333
    • 4644360265 scopus 로고    scopus 로고
    • The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin
    • Roche FM, Downer R, Keane F, Speziale P, Park PW & Foster TJ (2004) The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin. J Biol Chem 279: 38433-38440.
    • (2004) J Biol Chem , vol.279 , pp. 38433-38440
    • Roche, F.M.1    Downer, R.2    Keane, F.3    Speziale, P.4    Park, P.W.5    Foster, T.J.6
  • 335
    • 0038039279 scopus 로고    scopus 로고
    • Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesion YadA
    • Roggenkamp A, Ackermann N, Jacobi CA, Truelzsch K, Hoffmann H & Heesemann J (2003) Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesion YadA. J Bacteriol 18: 3735-3744.
    • (2003) J Bacteriol , vol.18 , pp. 3735-3744
    • Roggenkamp, A.1    Ackermann, N.2    Jacobi, C.A.3    Truelzsch, K.4    Hoffmann, H.5    Heesemann, J.6
  • 336
    • 0042978789 scopus 로고    scopus 로고
    • Host cell caveolae act as an entry-port for group A streptococci
    • Rohde M, Muller E, Chhatwal GS & Talay SR (2003) Host cell caveolae act as an entry-port for group A streptococci. Cell Microbiol 5: 323-342.
    • (2003) Cell Microbiol , vol.5 , pp. 323-342
    • Rohde, M.1    Muller, E.2    Chhatwal, G.S.3    Talay, S.R.4
  • 337
    • 0033960935 scopus 로고    scopus 로고
    • Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines
    • Ronning DR, Klabunde T, Besra GS, Vissa VD, Belisle JT & Sacchettini JC (2000) Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nature Struct Biol 7: 141-146.
    • (2000) Nature Struct Biol , vol.7 , pp. 141-146
    • Ronning, D.R.1    Klabunde, T.2    Besra, G.S.3    Vissa, V.D.4    Belisle, J.T.5    Sacchettini, J.C.6
  • 338
    • 29644444981 scopus 로고    scopus 로고
    • Members of the 30- to 32-kilodalton mycolyl transferase family (Ag85) from culture filtrate of Mycobacterium avium subsp. paratuberculosis are immunodominant Th1-type antigens recognized early upon infection in mice and cattle
    • Rosseels V, Marché S, Roupie V, Govaerts M, Godfroid J, Walravens K & Huygen K (2006) Members of the 30- to 32-kilodalton mycolyl transferase family (Ag85) from culture filtrate of Mycobacterium avium subsp. paratuberculosis are immunodominant Th1-type antigens recognized early upon infection in mice and cattle. Infect Immun 74: 202-212.
    • (2006) Infect Immun , vol.74 , pp. 202-212
    • Rosseels, V.1    Marché, S.2    Roupie, V.3    Govaerts, M.4    Godfroid, J.5    Walravens, K.6    Huygen, K.7
  • 341
    • 0019364733 scopus 로고
    • Comparative studies on amniotic fluid and plasma fibronectins
    • Ruoslahti E, Engvall E, Hayman EG & Spiro RG (1981a) Comparative studies on amniotic fluid and plasma fibronectins. Biochem J 193: 295-299.
    • (1981) Biochem J , vol.193 , pp. 295-299
    • Ruoslahti, E.1    Engvall, E.2    Hayman, E.G.3    Spiro, R.G.4
  • 344
    • 0032697555 scopus 로고    scopus 로고
    • The fibronectin extra domain A activates matrix metalloproteinase gene expression by an interleukin-1-dependent mechanism
    • Saito S, Yamaji N, Yasunaga K, Saito T, Matsumoto S, Katoh M, Kobayashi S & Masuho Y (1999) The fibronectin extra domain A activates matrix metalloproteinase gene expression by an interleukin-1-dependent mechanism. J Biol Chem 274: 30756-30763.
    • (1999) J Biol Chem , vol.274 , pp. 30756-30763
    • Saito, S.1    Yamaji, N.2    Yasunaga, K.3    Saito, T.4    Matsumoto, S.5    Katoh, M.6    Kobayashi, S.7    Masuho, Y.8
  • 345
    • 63849126614 scopus 로고    scopus 로고
    • Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli
    • Saldaña Z, Xicohtencatl-Cortes J, Avelino F, Phillips AD, Kaper JB, Puente JL & Girón JA (2009) Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli. Environ Microbiol 11: 992-1006.
    • (2009) Environ Microbiol , vol.11 , pp. 992-1006
    • Saldaña, Z.1    Xicohtencatl-Cortes, J.2    Avelino, F.3    Phillips, A.D.4    Kaper, J.B.5    Puente, J.L.6    Girón, J.A.7
  • 346
    • 66849103966 scopus 로고    scopus 로고
    • Identification of surface proteins involved in the adhesion of a probiotic Bacillus cereus strain to mucin and fibronectin
    • Sánchez B, Arias S, Chaignepain S, Denayrolles M, Schmitter JM, Bressollier P & Urdaci MC (2009) Identification of surface proteins involved in the adhesion of a probiotic Bacillus cereus strain to mucin and fibronectin. Microbiology 155: 1708-1716.
    • (2009) Microbiology , vol.155 , pp. 1708-1716
    • Sánchez, B.1    Arias, S.2    Chaignepain, S.3    Denayrolles, M.4    Schmitter, J.M.5    Bressollier, P.6    Urdaci, M.C.7
  • 348
    • 48349095742 scopus 로고    scopus 로고
    • Glycosylation and ligand-binding activities of rat plasma fibronectin during liver regeneration after partial hepatectomy
    • Sano K, Asahi M, Yanagibashi M, Hashii N, Itoh S, Kawasaki N & Ogawa H (2008) Glycosylation and ligand-binding activities of rat plasma fibronectin during liver regeneration after partial hepatectomy. Carbohydr Res 343: 2329-2335.
    • (2008) Carbohydr Res , vol.343 , pp. 2329-2335
    • Sano, K.1    Asahi, M.2    Yanagibashi, M.3    Hashii, N.4    Itoh, S.5    Kawasaki, N.6    Ogawa, H.7
  • 349
    • 0041196235 scopus 로고    scopus 로고
    • Transcription of Staphylococcus aureus fibronectin binding protein genes is negatively regulated by agr and an agr-independent mechanism
    • Saravia-Otten P, Muller HP & Arvidson S (1997) Transcription of Staphylococcus aureus fibronectin binding protein genes is negatively regulated by agr and an agr-independent mechanism. J Bacteriol 179: 5259-5263.
    • (1997) J Bacteriol , vol.179 , pp. 5259-5263
    • Saravia-Otten, P.1    Muller, H.P.2    Arvidson, S.3
  • 350
    • 0027501305 scopus 로고
    • Immunisation with fibronectin binding protein from Staphylococcus sureus protects rats against experimental endocarditis in rats
    • Schennings T, Heimdahl A, Coster K & Flock J-I (1993) Immunisation with fibronectin binding protein from Staphylococcus sureus protects rats against experimental endocarditis in rats. Microb Pathog 15: 227-236.
    • (1993) Microb Pathog , vol.15 , pp. 227-236
    • Schennings, T.1    Heimdahl, A.2    Coster, K.3    Flock, J.4
  • 351
    • 0027407983 scopus 로고
    • Adhesion of Lactobacillus acidophilus to avian intestinal epithelial cells mediated by the crystalline bacterial cell surface layer (S-layer)
    • Schneitz C, Nuotio L & Lounatmaa K (1993) Adhesion of Lactobacillus acidophilus to avian intestinal epithelial cells mediated by the crystalline bacterial cell surface layer (S-layer). J Appl Bacteriol 74: 290-294.
    • (1993) J Appl Bacteriol , vol.74 , pp. 290-294
    • Schneitz, C.1    Nuotio, L.2    Lounatmaa, K.3
  • 352
    • 0029070194 scopus 로고
    • A Mycobacterium leprae gene encoding a fibronectin binding protein is used for efficient invasion of epithelial cells and Schwann cells
    • Schorey JS, Li Q, McCourt DW, Bong-Mastek M, Clark-Curtiss JE, Ratliff TL & Brown EJ (1995) A Mycobacterium leprae gene encoding a fibronectin binding protein is used for efficient invasion of epithelial cells and Schwann cells. Infect Immun 63: 2652-2657.
    • (1995) Infect Immun , vol.63 , pp. 2652-2657
    • Schorey, J.S.1    Li, Q.2    McCourt, D.W.3    Bong-Mastek, M.4    Clark-Curtiss, J.E.5    Ratliff, T.L.6    Brown, E.J.7
  • 353
    • 0029784779 scopus 로고    scopus 로고
    • Characterization of the fibronectin-attachment protein of Mycobacterium avium reveals a fibronectin-binding motif among mycobacteria
    • Schorey JS, Holsti MA, Ratliff TL, Allen PM & Brown EJ (1996) Characterization of the fibronectin-attachment protein of Mycobacterium avium reveals a fibronectin-binding motif among mycobacteria. Mol Microbiol 21: 321-329.
    • (1996) Mol Microbiol , vol.21 , pp. 321-329
    • Schorey, J.S.1    Holsti, M.A.2    Ratliff, T.L.3    Allen, P.M.4    Brown, E.J.5
  • 354
    • 33845423107 scopus 로고    scopus 로고
    • Staphylococcus aureus fibronectin binding protein-A induces motile attachment sites and complex actin remodelling in living endothelial cells
    • Schroder A, Schroder B, Roppenser B, Linder S, Sinha B, Fassler R & Aepfelbacher M (2006) Staphylococcus aureus fibronectin binding protein-A induces motile attachment sites and complex actin remodelling in living endothelial cells. Mol Biol Cell 17: 5198-5210.
    • (2006) Mol Biol Cell , vol.17 , pp. 5198-5210
    • Schroder, A.1    Schroder, B.2    Roppenser, B.3    Linder, S.4    Sinha, B.5    Fassler, R.6    Aepfelbacher, M.7
  • 355
    • 0027232623 scopus 로고
    • Outer membrane protein YadA of enteropathogenic yersiniae mediates specific binding to cellular but not plasma fibronectin
    • Schulze-Koops H, Burkhardt H, Heesemann J, Kirsch T, Swoboda B, Bull C, Goodman S & Emmrich F (1993) Outer membrane protein YadA of enteropathogenic yersiniae mediates specific binding to cellular but not plasma fibronectin. Infect Immun 61: 2513-2519.
    • (1993) Infect Immun , vol.61 , pp. 2513-2519
    • Schulze-Koops, H.1    Burkhardt, H.2    Heesemann, J.3    Kirsch, T.4    Swoboda, B.5    Bull, C.6    Goodman, S.7    Emmrich, F.8
  • 357
    • 2442442058 scopus 로고    scopus 로고
    • The molecular basis of fibronectin-mediated bacterial adherence to host cells
    • Schwarz-Linek U, Hook M & Potts JR (2004) The molecular basis of fibronectin-mediated bacterial adherence to host cells. Mol Microbiol 52: 631-641.
    • (2004) Mol Microbiol , vol.52 , pp. 631-641
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 358
    • 33748209542 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of Gram-positive cocci
    • Schwarz-Linek U, Hook M & Potts JR (2006) Fibronectin-binding proteins of Gram-positive cocci. Microbes Infect 8: 2291-2298.
    • (2006) Microbes Infect , vol.8 , pp. 2291-2298
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 359
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequence required for assembly of a fibrillar matrix
    • Schwarzbauer JE (1991) Identification of the fibronectin sequence required for assembly of a fibrillar matrix. J Cell Biol 113: 1463-1473.
    • (1991) J Cell Biol , vol.113 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 360
    • 0021042241 scopus 로고
    • Three different fibronectin RNAs arise by alternative splicing within the coding region
    • Schwarzbauer JE, Tamkun JW, Lemischka IR & Hynes RO (1983) Three different fibronectin RNAs arise by alternative splicing within the coding region. Cell 35: 421-431.
    • (1983) Cell , vol.35 , pp. 421-431
    • Schwarzbauer, J.E.1    Tamkun, J.W.2    Lemischka, I.R.3    Hynes, R.O.4
  • 361
    • 76749149598 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding
    • Scott NE, Marzook NB, Deutscher A, Falconer L, Crossett B, Djordjevic SP & Cordwell SJ (2010) Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding. Proteomics 10: 277-288.
    • (2010) Proteomics , vol.10 , pp. 277-288
    • Scott, N.E.1    Marzook, N.B.2    Deutscher, A.3    Falconer, L.4    Crossett, B.5    Djordjevic, S.P.6    Cordwell, S.J.7
  • 363
    • 60349114577 scopus 로고    scopus 로고
    • Staphylococcus aureus as an intracellular pathogen
    • Trends Microbiol
    • Sendi P & Proctor RA (2009) Staphylococcus aureus as an intracellular pathogen: the role of small colony variants. Trends Microbiol 17: 54-58.
    • (2009) the role of small colony variants , vol.17 , pp. 54-58
    • Sendi, P.1    Proctor, R.A.2
  • 364
    • 33645092915 scopus 로고    scopus 로고
    • Inactivation of the fibronectin-binding adhesion gene bbk32 significantly attenuates the infectivity potential of Borrelia burgdorferi
    • Seshu J, Esteve-Gassent MD, Labandeire-Rey M, Kim JH, Trzeciakowski JP, Hook M & Skare JT (2006) Inactivation of the fibronectin-binding adhesion gene bbk32 significantly attenuates the infectivity potential of Borrelia burgdorferi. Mol Microbiol 59: 1591-1601.
    • (2006) Mol Microbiol , vol.59 , pp. 1591-1601
    • Seshu, J.1    Esteve-Gassent, M.D.2    Labandeire-Rey, M.3    Kim, J.H.4    Trzeciakowski, J.P.5    Hook, M.6    Skare, J.T.7
  • 365
    • 0344009684 scopus 로고    scopus 로고
    • Role of toll-like receptors and their adapters in adjuvant immunotherapy for cancer
    • Seya T, Akazawa T, Uehori J, Matsumoto M, Azuma I & Toyoshima K (2003) Role of toll-like receptors and their adapters in adjuvant immunotherapy for cancer. Anticancer Res 23: 4369-4376.
    • (2003) Anticancer Res , vol.23 , pp. 4369-4376
    • Seya, T.1    Akazawa, T.2    Uehori, J.3    Matsumoto, M.4    Azuma, I.5    Toyoshima, K.6
  • 366
    • 0031797896 scopus 로고    scopus 로고
    • Cloning, expression, and sequencing of a cell surface antigen containing a leucine-rich repeat motif from Bacteroides forsythus ATCC 43037
    • Sharma A, Sojar HT, Glurich I, Honma K, Kuramitsu HK & Genco RJ (1998) Cloning, expression, and sequencing of a cell surface antigen containing a leucine-rich repeat motif from Bacteroides forsythus ATCC 43037. Infect Immun 66: 5703-5710.
    • (1998) Infect Immun , vol.66 , pp. 5703-5710
    • Sharma, A.1    Sojar, H.T.2    Glurich, I.3    Honma, K.4    Kuramitsu, H.K.5    Genco, R.J.6
  • 367
    • 0033559259 scopus 로고    scopus 로고
    • Crystal structure of a heparin and integrin-binding segment of human fibronectin
    • Sharma A, Askari JA, Humphries MJ, Jones EY & Stuart DI (1999) Crystal structure of a heparin and integrin-binding segment of human fibronectin. EMBO J 18: 1468-1479.
    • (1999) EMBO J , vol.18 , pp. 1468-1479
    • Sharma, A.1    Askari, J.A.2    Humphries, M.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 368
    • 49649095969 scopus 로고    scopus 로고
    • Caveolin-1 dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover
    • Shi F & Sottile J (2008) Caveolin-1 dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover. J Cell Sci 121: 2360-2371.
    • (2008) J Cell Sci , vol.121 , pp. 2360-2371
    • Shi, F.1    Sottile, J.2
  • 369
    • 0037408416 scopus 로고    scopus 로고
    • Adhesive surface proteins of Erysipelothrix rhusopathiae bind to polystyrene, fibronectin and types I and IV collagen
    • Shimoji Y, Ogawa Y, Osaki M, Kabeya H, Maruyama S, Mikami T & Sekizaki T (2003) Adhesive surface proteins of Erysipelothrix rhusopathiae bind to polystyrene, fibronectin and types I and IV collagen. J Bacteriol 185: 2739-2748.
    • (2003) J Bacteriol , vol.185 , pp. 2739-2748
    • Shimoji, Y.1    Ogawa, Y.2    Osaki, M.3    Kabeya, H.4    Maruyama, S.5    Mikami, T.6    Sekizaki, T.7
  • 370
    • 0032420365 scopus 로고    scopus 로고
    • Different effects of fibronectin on the phagocytosis of Staphylococcus aureus and coagulase-negative staphylococci by murine peritoneal macrophages
    • Shinji H, Sakurada J, Seki K, Murai M & Masuda S (1998) Different effects of fibronectin on the phagocytosis of Staphylococcus aureus and coagulase-negative staphylococci by murine peritoneal macrophages. Microbiol Immunol 42: 851-861.
    • (1998) Microbiol Immunol , vol.42 , pp. 851-861
    • Shinji, H.1    Sakurada, J.2    Seki, K.3    Murai, M.4    Masuda, S.5
  • 371
    • 33846496189 scopus 로고    scopus 로고
    • Expression and distribution of very late antigen-5 in mouse peritoneal macrophages upon ingestion of fibronectin-bound Staphylococcus aureus
    • Shinji H, Kamada M, Seki K, Tajima A, Iwase T & Masuda S (2007) Expression and distribution of very late antigen-5 in mouse peritoneal macrophages upon ingestion of fibronectin-bound Staphylococcus aureus. Microbiol Immunol 51: 63-71.
    • (2007) Microbiol Immunol , vol.51 , pp. 63-71
    • Shinji, H.1    Kamada, M.2    Seki, K.3    Tajima, A.4    Iwase, T.5    Masuda, S.6
  • 372
    • 55949090817 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni proteins recognized by maternal antibodies of chickens
    • Shoaf-Sweeney KD, Larson CL, Tang X & Konkel ME (2008) Identification of Campylobacter jejuni proteins recognized by maternal antibodies of chickens. Appl Environ Microb 74: 6867-6875.
    • (2008) Appl Environ Microb , vol.74 , pp. 6867-6875
    • Shoaf-Sweeney, K.D.1    Larson, C.L.2    Tang, X.3    Konkel, M.E.4
  • 374
    • 55549148430 scopus 로고    scopus 로고
    • Identification and phenotypic characterization of a second collagen adhesin, Scm, and genome-based identification and analysis of 13 other predicted MSCRAMMs, including four distinct pilus loci, in Enterococcus faecium
    • Sillanpää J, Nallapareddy SR, Prakash VP, Qin X, Höök M, Weinstock GM & Murray BE (2008) Identification and phenotypic characterization of a second collagen adhesin, Scm, and genome-based identification and analysis of 13 other predicted MSCRAMMs, including four distinct pilus loci, in Enterococcus faecium. Microbiology 154: 3199-3211.
    • (2008) Microbiology , vol.154 , pp. 3199-3211
    • Sillanpää, J.1    Nallapareddy, S.R.2    Prakash, V.P.3    Qin, X.4    Höök, M.5    Weinstock, G.M.6    Murray, B.E.7
  • 377
  • 378
    • 33644816813 scopus 로고    scopus 로고
    • The influence of adhesive and invasive properties of Staphylococcus aureus defective in fibronectin-binding protins on secretion or interleukin-6 by human endothelial cells
    • Soderquist B, Alriksson I, Kallman J & Kihlstrom E (2006) The influence of adhesive and invasive properties of Staphylococcus aureus defective in fibronectin-binding protins on secretion or interleukin-6 by human endothelial cells. APMIS 114: 112-116.
    • (2006) APMIS , vol.114 , pp. 112-116
    • Soderquist, B.1    Alriksson, I.2    Kallman, J.3    Kihlstrom, E.4
  • 382
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerisation regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • Sottile J & Hocking DC (2002) Fibronectin polymerisation regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol Biol Cell 13: 3546-3559.
    • (2002) Mol Biol Cell , vol.13 , pp. 3546-3559
    • Sottile, J.1    Hocking, D.C.2
  • 383
    • 12844269776 scopus 로고    scopus 로고
    • Fibronectin matrix turnover occurs through a caveolin-1-dependent process
    • Sottile J & Chandler J (2005) Fibronectin matrix turnover occurs through a caveolin-1-dependent process. Mol Cell Biol 16: 757-768.
    • (2005) Mol Cell Biol , vol.16 , pp. 757-768
    • Sottile, J.1    Chandler, J.2
  • 384
    • 0028857075 scopus 로고
    • The OmpU outer membrane protein, a potential virulence factor of Vibrio cholera
    • Sperandio V, Girón JA, Silveira WD & Kaper JB (1995) The OmpU outer membrane protein, a potential virulence factor of Vibrio cholera. Infect Immun 63: 4433-4438.
    • (1995) Infect Immun , vol.63 , pp. 4433-4438
    • Sperandio, V.1    Girón, J.A.2    Silveira, W.D.3    Kaper, J.B.4
  • 385
    • 0030050844 scopus 로고    scopus 로고
    • A monoclonal antibody enhances ligand binding of fibronectin MSCRAMM (adhesin) from Streptococcus dysgalactiae
    • Speziale P, Joh D, Visai L, Bozzini S, House-Pompeo K, Lindberg M & Höök M (1996) A monoclonal antibody enhances ligand binding of fibronectin MSCRAMM (adhesin) from Streptococcus dysgalactiae. J Biol Chem 271: 1371-1378.
    • (1996) J Biol Chem , vol.271 , pp. 1371-1378
    • Speziale, P.1    Joh, D.2    Visai, L.3    Bozzini, S.4    House-Pompeo, K.5    Lindberg, M.6    Höök, M.7
  • 388
    • 65249094939 scopus 로고    scopus 로고
    • Preparation of recombinant fibronectin fragments for functional and structural studies
    • Staunton D, Millard CJ, Aricescu AR & Campbell ID (2009) Preparation of recombinant fibronectin fragments for functional and structural studies. Methods Mol Biol 522: 1-27.
    • (2009) Methods Mol Biol , vol.522 , pp. 1-27
    • Staunton, D.1    Millard, C.J.2    Aricescu, A.R.3    Campbell, I.D.4
  • 389
    • 43149110212 scopus 로고    scopus 로고
    • Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement
    • Stevenson B, Choy HA, Pinne M et al. (2007) Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. PLoS ONE 2: e1188.
    • (2007) PLoS ONE , vol.2
    • Stevenson, B.1    Choy, H.A.2    Pinne, M.3
  • 390
    • 0036230874 scopus 로고    scopus 로고
    • Molecular and cellular determinants of non-typeable Haemophilus influenza adherence and invasion
    • St Geme JW (2002) Molecular and cellular determinants of non-typeable Haemophilus influenza adherence and invasion. Cell Microbiol 4: 191-200.
    • (2002) Cell Microbiol , vol.4 , pp. 191-200
    • St Geme, J.W.1
  • 391
    • 0032512876 scopus 로고    scopus 로고
    • Solution structure of the glycosylated second type 2 module of fibronectin
    • Sticht H, Pickford AR, Potts JR & Campbell ID (1998) Solution structure of the glycosylated second type 2 module of fibronectin. J Mol Biol 276: 177-187.
    • (1998) J Mol Biol , vol.276 , pp. 177-187
    • Sticht, H.1    Pickford, A.R.2    Potts, J.R.3    Campbell, I.D.4
  • 392
    • 4644299670 scopus 로고    scopus 로고
    • Mode of binding of fibrinogen, fibronectin and iron-binding proteins by animal enterococci
    • Styriak I, Laukova A, Strompfova V & Ljungh A (2004) Mode of binding of fibrinogen, fibronectin and iron-binding proteins by animal enterococci. Vet Res Commun 28: 587-598.
    • (2004) Vet Res Commun , vol.28 , pp. 587-598
    • Styriak, I.1    Laukova, A.2    Strompfova, V.3    Ljungh, A.4
  • 394
    • 66049089710 scopus 로고    scopus 로고
    • Determination of fibronectin-binding region of FBPS of Streptococcus suis type 2
    • Sun LY, Fan HJ & Lu CP (2005) Determination of fibronectin-binding region of FBPS of Streptococcus suis type 2. Wei Sheng Wu Xue Bao 45: 753-756.
    • (2005) Wei Sheng Wu Xue Bao , vol.45 , pp. 753-756
    • Sun, L.Y.1    Fan, H.J.2    Lu, C.P.3
  • 395
    • 0020434630 scopus 로고
    • Binding of fibronectin to the surface of group A, C, and G streptococci isolated from human infections
    • Switalski LM, Ljungh A, Ryden C, Rubin K, Hook M & Wadstrom T (1982) Binding of fibronectin to the surface of group A, C, and G streptococci isolated from human infections. Eur J Clin Microbiol 1: 381-387.
    • (1982) Eur J Clin Microbiol , vol.1 , pp. 381-387
    • Switalski, L.M.1    Ljungh, A.2    Ryden, C.3    Rubin, K.4    Hook, M.5    Wadstrom, T.6
  • 398
    • 0025879657 scopus 로고
    • Expression of the fibronectin-binding components of Streptococcus pyogenes in Escherichia coli demonstrates that they are proteins
    • Talay SR, Ehrenfeld E, Chhatwal GS & Timmis KN (1991) Expression of the fibronectin-binding components of Streptococcus pyogenes in Escherichia coli demonstrates that they are proteins. Mol Microbiol 5: 1727-1734.
    • (1991) Mol Microbiol , vol.5 , pp. 1727-1734
    • Talay, S.R.1    Ehrenfeld, E.2    Chhatwal, G.S.3    Timmis, K.N.4
  • 400
    • 0034524338 scopus 로고    scopus 로고
    • Co-operative binding of human fibronectin to Sfbl protein triggers streptococcal invasion into respiratory epithelial cells
    • Talay SR, Zock A, Rohde M, Molinari G, Oggioni M, Pozzi G, Guzman CA & Chhatwal GS (2000) Co-operative binding of human fibronectin to Sfbl protein triggers streptococcal invasion into respiratory epithelial cells. Cell Microbiol 2: 521-535.
    • (2000) Cell Microbiol , vol.2 , pp. 521-535
    • Talay, S.R.1    Zock, A.2    Rohde, M.3    Molinari, G.4    Oggioni, M.5    Pozzi, G.6    Guzman, C.A.7    Chhatwal, G.S.8
  • 401
    • 33749257523 scopus 로고    scopus 로고
    • High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity
    • Tamura GS, Hull JR, Oberg MD & Castner DG (2006) High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity. Infect Immun 74: 5739-5746.
    • (2006) Infect Immun , vol.74 , pp. 5739-5746
    • Tamura, G.S.1    Hull, J.R.2    Oberg, M.D.3    Castner, D.G.4
  • 403
    • 0042825455 scopus 로고    scopus 로고
    • An Enterococcus faecium secreted antigen, SagA, exhibits broad-spectrum binding to extracellular matrix proteins and appears essential for E. faecium growth
    • Teng F, Kawalec M, Weinstock GM, Hyrniewicz W & Murray BE (2003) An Enterococcus faecium secreted antigen, SagA, exhibits broad-spectrum binding to extracellular matrix proteins and appears essential for E. faecium growth. Infect Immun 71: 5033-5041.
    • (2003) Infect Immun , vol.71 , pp. 5033-5041
    • Teng, F.1    Kawalec, M.2    Weinstock, G.M.3    Hyrniewicz, W.4    Murray, B.E.5
  • 404
    • 0035724292 scopus 로고    scopus 로고
    • Fba, a novel fibronectin-binding protein from Streptococcus pyogenes, promotes bacterial entry into epithelial cells, and the fba gene is positively transcribed under the Mga regulator
    • Terao Y, Kawabata S, Kunitomo E, Murakami J, Nakagawa I & Hamada S (2001) Fba, a novel fibronectin-binding protein from Streptococcus pyogenes, promotes bacterial entry into epithelial cells, and the fba gene is positively transcribed under the Mga regulator. Mol Microbiol 42: 75-86.
    • (2001) Mol Microbiol , vol.42 , pp. 75-86
    • Terao, Y.1    Kawabata, S.2    Kunitomo, E.3    Murakami, J.4    Nakagawa, I.5    Hamada, S.6
  • 405
    • 0037033063 scopus 로고    scopus 로고
    • Molecular characterization of a novel fibronectin-binding protein of Streptococcus pyogenes strains isolated from toxic shock-like syndrome patients
    • Terao Y, Kawabata S, Nakata M, Nakagawa I & Hamada S (2002) Molecular characterization of a novel fibronectin-binding protein of Streptococcus pyogenes strains isolated from toxic shock-like syndrome patients. J Biol Chem 277: 47428-47435.
    • (2002) J Biol Chem , vol.277 , pp. 47428-47435
    • Terao, Y.1    Kawabata, S.2    Nakata, M.3    Nakagawa, I.4    Hamada, S.5
  • 406
    • 28844485361 scopus 로고    scopus 로고
    • Protective immunity against Streptococcus pyogenes challenge in mice after immunization with fibronectin-binding protein
    • Terao Y, Okamoto S, Kataoka K, Hamada S & Kawabata S (2005) Protective immunity against Streptococcus pyogenes challenge in mice after immunization with fibronectin-binding protein. J Infect Dis 192: 2081-2091.
    • (2005) J Infect Dis , vol.192 , pp. 2081-2091
    • Terao, Y.1    Okamoto, S.2    Kataoka, K.3    Hamada, S.4    Kawabata, S.5
  • 407
    • 0026650357 scopus 로고
    • Adhesion protein YadA of Yersinia species mediate binding of bacteria to fibronectin
    • Tertti R, Skurnik M, Vartio T & Kuusela P (1992) Adhesion protein YadA of Yersinia species mediate binding of bacteria to fibronectin. Infect Immun 60: 3021-3024.
    • (1992) Infect Immun , vol.60 , pp. 3021-3024
    • Tertti, R.1    Skurnik, M.2    Vartio, T.3    Kuusela, P.4
  • 408
    • 0021945840 scopus 로고
    • Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain
    • Thomas DD, Baseman JB & Alderete JF (1985a) Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain. J Exp Med 161: 514-525.
    • (1985) J Exp Med , vol.161 , pp. 514-525
    • Thomas, D.D.1    Baseman, J.B.2    Alderete, J.F.3
  • 409
    • 0022407510 scopus 로고
    • Fibronectin tetrapeptide is target for syphilis spirochete cytadherence
    • Thomas DD, Baseman JB & Alderete JF (1985b) Fibronectin tetrapeptide is target for syphilis spirochete cytadherence. J Exp Med 162: 1715-1719.
    • (1985) J Exp Med , vol.162 , pp. 1715-1719
    • Thomas, D.D.1    Baseman, J.B.2    Alderete, J.F.3
  • 410
    • 0021861545 scopus 로고
    • Putative Treponema pallidum cytoadhesins share a common functional domain
    • Thomas DD, Baseman JB & Alderete JF (1985c) Putative Treponema pallidum cytoadhesins share a common functional domain. Infect Immun 49: 833-835.
    • (1985) Infect Immun , vol.49 , pp. 833-835
    • Thomas, D.D.1    Baseman, J.B.2    Alderete, J.F.3
  • 413
    • 0032063303 scopus 로고    scopus 로고
    • Presence of a fibronectin type III domain in a plant protein
    • Tsyguelnaia I & Doolittle RF (1998) Presence of a fibronectin type III domain in a plant protein. J Mol Evol 46: 612-624.
    • (1998) J Mol Evol , vol.46 , pp. 612-624
    • Tsyguelnaia, I.1    Doolittle, R.F.2
  • 414
    • 0037151078 scopus 로고    scopus 로고
    • The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin
    • Tu H, Sasaki T, Snellman A, Göhring W, Pirilä P, Timpl R & Pihlajaniemi T (2002) The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin. J Biol Chem 277: 23092-23099.
    • (2002) J Biol Chem , vol.277 , pp. 23092-23099
    • Tu, H.1    Sasaki, T.2    Snellman, A.3    Göhring, W.4    Pirilä, P.5    Timpl, R.6    Pihlajaniemi, T.7
  • 415
    • 77449117998 scopus 로고    scopus 로고
    • Calcium binds to LipL32, a lipoprotein from pathogenic Leptospira, and modulates fibronectin binding
    • Tung JY, Yang CW, Chou SW, Lin CC & Sun YJ (2010) Calcium binds to LipL32, a lipoprotein from pathogenic Leptospira, and modulates fibronectin binding. J Biol Chem 285: 3245-3252.
    • (2010) J Biol Chem , vol.285 , pp. 3245-3252
    • Tung, J.Y.1    Yang, C.W.2    Chou, S.W.3    Lin, C.C.4    Sun, Y.J.5
  • 416
    • 0027531601 scopus 로고
    • Fibronectin binding proteins of a human oral spirochaete, Treponema denticola
    • Umemoto T, Nakatani Y, Nakamura Y & Namikawa I (1993) Fibronectin binding proteins of a human oral spirochaete, Treponema denticola. Microbiol Immunol 37: 75-78.
    • (1993) Microbiol Immunol , vol.37 , pp. 75-78
    • Umemoto, T.1    Nakatani, Y.2    Nakamura, Y.3    Namikawa, I.4
  • 421
    • 0031871416 scopus 로고    scopus 로고
    • + gonococci into Hep-2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors
    • + gonococci into Hep-2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors. Mol Microbiol 29: 369-379.
    • (1998) Mol Microbiol , vol.29 , pp. 369-379
    • Van Putten, J.P.1    Duensing, T.D.2    Cole, R.L.3
  • 425
    • 0033801642 scopus 로고    scopus 로고
    • Interaction of fimbriae of Haemophilus influenza type B with heparin-binding extracellular matrix proteins
    • Virkola R, Brummer M, Rauvala H, Van Alphen L & Korhonen TK (2000) Interaction of fimbriae of Haemophilus influenza type B with heparin-binding extracellular matrix proteins. Infect Immun 68: 5696-5701.
    • (2000) Infect Immun , vol.68 , pp. 5696-5701
    • Virkola, R.1    Brummer, M.2    Rauvala, H.3    Van Alphen, L.4    Korhonen, T.K.5
  • 426
    • 0025850470 scopus 로고
    • Binding sites in fibronectin for an enterotoxigenic strains of E. coli B3242289c
    • Visai L, Bozzini S, Petersen TE, Speziale L & Speziale P (1991) Binding sites in fibronectin for an enterotoxigenic strains of E. coli B3242289c. FEBS Lett 290: 111-114.
    • (1991) FEBS Lett , vol.290 , pp. 111-114
    • Visai, L.1    Bozzini, S.2    Petersen, T.E.3    Speziale, L.4    Speziale, P.5
  • 428
    • 4544223092 scopus 로고    scopus 로고
    • Polarized fibronectin secretion induced by adenosine regulates bacterial-epithelial interaction in human intestinal epithelial cells
    • Walia B, Castaneda FE, Wang L, Kolachala VL, Bajaj R, Roman J, Merlin D, Gewirtz AT & Sitaraman SV (2004) Polarized fibronectin secretion induced by adenosine regulates bacterial-epithelial interaction in human intestinal epithelial cells. Biochem J 383: 589-596.
    • (2004) Biochem J , vol.383 , pp. 589-596
    • Walia, B.1    Castaneda, F.E.2    Wang, L.3    Kolachala, V.L.4    Bajaj, R.5    Roman, J.6    Merlin, D.7    Gewirtz, A.T.8    Sitaraman, S.V.9
  • 430
    • 0034607985 scopus 로고    scopus 로고
    • The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen
    • Wann ER, Gurusiddappa S & Hook M (2000) The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen. J Biol Chem 275: 13863-13871.
    • (2000) J Biol Chem , vol.275 , pp. 13863-13871
    • Wann, E.R.1    Gurusiddappa, S.2    Hook, M.3
  • 431
    • 0014936515 scopus 로고
    • Differences between streptococcal infections of the throat and of the skin (second of two parts)
    • Wannamaker LW (1970) Differences between streptococcal infections of the throat and of the skin (second of two parts). N Engl J Med 282: 78-85.
    • (1970) N Engl J Med , vol.282 , pp. 78-85
    • Wannamaker, L.W.1
  • 434
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs or fibronectin matrix assembly
    • Wierzbicka-Patynowski I & Schwarzbauer JE (2003) The ins and outs or fibronectin matrix assembly. J Cell Sci 116: 3269-3276.
    • (2003) J Cell Sci , vol.116 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 435
    • 0037067431 scopus 로고    scopus 로고
    • Novel vascular endothelial growth factor binding domains of fibronectin enhance vascular endothelial growth factor biological activity
    • Wijelath ES, Murray J, Rahman S et al. (2002) Novel vascular endothelial growth factor binding domains of fibronectin enhance vascular endothelial growth factor biological activity. Circ Res 91: 25-31.
    • (2002) Circ Res , vol.91 , pp. 25-31
    • Wijelath, E.S.1    Murray, J.2    Rahman, S.3
  • 437
    • 0028213715 scopus 로고    scopus 로고
    • Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity
    • Williams MJ, Phan I, Harvey TS, Rostagno A, Gold LI & Campbell ID (1998) Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity. J Mol Biol 235: 1302-1311.
    • (1998) J Mol Biol , vol.235 , pp. 1302-1311
    • Williams, M.J.1    Phan, I.2    Harvey, T.S.3    Rostagno, A.4    Gold, L.I.5    Campbell, I.D.6
  • 438
    • 0036579594 scopus 로고    scopus 로고
    • Staphylococcus aureus fibronectin binding proteins A and B possess a second fibronectin binding region that may have biological relevance to bone tissues
    • Williams RJ, Henderson B & Nair SP (2002a) Staphylococcus aureus fibronectin binding proteins A and B possess a second fibronectin binding region that may have biological relevance to bone tissues. Calcif Tissue Int 70: 416-421.
    • (2002) Calcif Tissue Int , vol.70 , pp. 416-421
    • Williams, R.J.1    Henderson, B.2    Nair, S.P.3
  • 439
    • 0036892212 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding protein from Staphylococcus epidermidis
    • Williams RJ, Henderson B, Sharp LJ & Nair SP (2002b) Identification of a fibronectin-binding protein from Staphylococcus epidermidis. Infect Immun 70: 6805-6810.
    • (2002) Infect Immun , vol.70 , pp. 6805-6810
    • Williams, R.J.1    Henderson, B.2    Sharp, L.J.3    Nair, S.P.4
  • 440
    • 0242627835 scopus 로고    scopus 로고
    • Bacterial Adhesion to Host Tissues: Mechanisms and Consequences
    • Cambridge University Press, Cambridge.
    • Wilson M (2002) Bacterial Adhesion to Host Tissues: Mechanisms and Consequences. Cambridge University Press, Cambridge.
    • (2002)
    • Wilson, M.1
  • 441
    • 0003900480 scopus 로고    scopus 로고
    • Bacterial Disease Mechanisms: An Introduction to Cellular Microbiology
    • Cambridge University Press, Cambridge.
    • Wilson M, McNab R & Henderson B (2002) Bacterial Disease Mechanisms: An Introduction to Cellular Microbiology. Cambridge University Press, Cambridge.
    • (2002)
    • Wilson, M.1    McNab, R.2    Henderson, B.3
  • 442
    • 0346996696 scopus 로고    scopus 로고
    • The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic α/β hydrolases
    • Wilson RA, Maughan WN, Kremer L, Besra GS & Futterer K (2004) The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic α/β hydrolases. J Mol Biol 335: 519-530.
    • (2004) J Mol Biol , vol.335 , pp. 519-530
    • Wilson, R.A.1    Maughan, W.N.2    Kremer, L.3    Besra, G.S.4    Futterer, K.5
  • 443
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeleton interaction are essential for the assembly of the fibronectin matrix
    • Wu C, Keiven VM, O'Toole TE, McDonald JA & Ginsberg MH (1995) Integrin activation and cytoskeleton interaction are essential for the assembly of the fibronectin matrix. Cell 83: 715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keiven, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 445
    • 0035022986 scopus 로고    scopus 로고
    • Molecular strategies for fimbrial expression and assembly
    • Wu H & Fives-Taylor PM (2001) Molecular strategies for fimbrial expression and assembly. Crit Rev Oral Biol Med 12: 101-115.
    • (2001) Crit Rev Oral Biol Med , vol.12 , pp. 101-115
    • Wu, H.1    Fives-Taylor, P.M.2
  • 446
    • 58149520023 scopus 로고    scopus 로고
    • The type IV pili of enterohemorrhagic Escherichia coli H7:0157are multipurpose structures with pathogenic attributes
    • Xicohtencatl-Cortes J, Monteiro-Neto V, Saldaña Z, Ledesma MA, Puente JL & Girón JA (2009) The type IV pili of enterohemorrhagic Escherichia coli H7:0157are multipurpose structures with pathogenic attributes. J Bacteriol 191: 411-421.
    • (2009) J Bacteriol , vol.191 , pp. 411-421
    • Xicohtencatl-Cortes, J.1    Monteiro-Neto, V.2    Saldaña, Z.3    Ledesma, M.A.4    Puente, J.L.5    Girón, J.A.6
  • 448
    • 61349132103 scopus 로고    scopus 로고
    • PfbA, a novel plasmin- and fibronectin-binding protein of Streptococcus pneumoniae contributes to fibronectin-dependent adhesion and antiphagocytosis
    • Yamaguchi M, Terao Y, Mori Y, Hamada S & Kawabata S (2008) PfbA, a novel plasmin- and fibronectin-binding protein of Streptococcus pneumoniae contributes to fibronectin-dependent adhesion and antiphagocytosis. J Biol Chem 283: 36272-36279.
    • (2008) J Biol Chem , vol.283 , pp. 36272-36279
    • Yamaguchi, M.1    Terao, Y.2    Mori, Y.3    Hamada, S.4    Kawabata, S.5
  • 450
    • 0036154488 scopus 로고    scopus 로고
    • Repression of the Staphylococcus aureus accessory gene regulator in serum and in vivo
    • Yarwood JM, McCormick JK, Paustian ML, Kapur V & Schlievert PM (2002) Repression of the Staphylococcus aureus accessory gene regulator in serum and in vivo. J Bacteriol 184: 1095-1101.
    • (2002) J Bacteriol , vol.184 , pp. 1095-1101
    • Yarwood, J.M.1    McCormick, J.K.2    Paustian, M.L.3    Kapur, V.4    Schlievert, P.M.5
  • 451
    • 33845193927 scopus 로고    scopus 로고
    • Identification and characterisation of a cell surface protein of Prevotella intermedia 17 with broad spectrum binding activity for extracellular matrix proteins
    • Yu F, Iyer D, Anaya C & Lewis JP (2006) Identification and characterisation of a cell surface protein of Prevotella intermedia 17 with broad spectrum binding activity for extracellular matrix proteins. Proteomics 6: 6023-6032.
    • (2006) Proteomics , vol.6 , pp. 6023-6032
    • Yu, F.1    Iyer, D.2    Anaya, C.3    Lewis, J.P.4
  • 453
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E & Geiger B (2001) Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci 114: 3583-3590.
    • (2001) J Cell Sci , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 454
    • 0344585468 scopus 로고    scopus 로고
    • Fibronectin-associated Fas ligand rapidly induces opposing and time-dependent effects on the activation and apoptosis of T cells
    • Zanin-Zorov A, Hershkoviz R, Hecht I, Cahalon L & Lider O (2003) Fibronectin-associated Fas ligand rapidly induces opposing and time-dependent effects on the activation and apoptosis of T cells. J Immunol 171: 5882-5889.
    • (2003) J Immunol , vol.171 , pp. 5882-5889
    • Zanin-Zorov, A.1    Hershkoviz, R.2    Hecht, I.3    Cahalon, L.4    Lider, O.5
  • 456
    • 0033582493 scopus 로고    scopus 로고
    • Characterization of the fibronectin binding motif for a unique mycobacterial fibronectin attachment protein, FAP
    • Zhao W, Schorey JS, Groger R, Allen PM, Brown EJ & Ratliff TL (1999) Characterization of the fibronectin binding motif for a unique mycobacterial fibronectin attachment protein, FAP. J Biol Chem 274: 4521-4526.
    • (1999) J Biol Chem , vol.274 , pp. 4521-4526
    • Zhao, W.1    Schorey, J.S.2    Groger, R.3    Allen, P.M.4    Brown, E.J.5    Ratliff, T.L.6
  • 457
    • 0034049176 scopus 로고    scopus 로고
    • Role of bacillus Calmette-Guerin fibronectin attachment protein in BCG-induced antitumor activity
    • Zhao W, Schorey JS, Bon-Mastek M, Ritchey J, Brown EJ & Ratliff TL (2000) Role of bacillus Calmette-Guerin fibronectin attachment protein in BCG-induced antitumor activity. Int J Cancer 86: 83-88.
    • (2000) Int J Cancer , vol.86 , pp. 83-88
    • Zhao, W.1    Schorey, J.S.2    Bon-Mastek, M.3    Ritchey, J.4    Brown, E.J.5    Ratliff, T.L.6
  • 458
    • 33646848449 scopus 로고    scopus 로고
    • An immunogenicity study of a newly fusion protein Cna-FnBP vaccinated against Staphylococcus sureus infections in a mice model
    • Zhou H, Xiong Z-Y, Li H-P, Zheng Y-L & Jiang Y-Q (2006) An immunogenicity study of a newly fusion protein Cna-FnBP vaccinated against Staphylococcus sureus infections in a mice model. Vaccine 24: 4830-4837.
    • (2006) Vaccine , vol.24 , pp. 4830-4837
    • Zhou, H.1    Xiong, Z.2    Li, H.3    Zheng, Y.4    Jiang, Y.5
  • 459
    • 0037369939 scopus 로고    scopus 로고
    • Hemin binding, functional expression and complementation analysis of Pap31 from Bartonella henselae
    • Zimmermann R, Kempf V, Schiltz E, Oberle K & Sander A (2003) Hemin binding, functional expression and complementation analysis of Pap31 from Bartonella henselae. J Bacteriol 185: 1739-1744.
    • (2003) J Bacteriol , vol.185 , pp. 1739-1744
    • Zimmermann, R.1    Kempf, V.2    Schiltz, E.3    Oberle, K.4    Sander, A.5
  • 460
    • 0033167220 scopus 로고    scopus 로고
    • The absence of cecal colonisation by a mutant of Campylobacter jejuni not expressing bacterial fibronectin binding protein
    • Ziprin RL, Young CR, Hume ME & Konkel ME (1999) The absence of cecal colonisation by a mutant of Campylobacter jejuni not expressing bacterial fibronectin binding protein. Avian Dis 43: 586-589.
    • (1999) Avian Dis , vol.43 , pp. 586-589
    • Ziprin, R.L.1    Young, C.R.2    Hume, M.E.3    Konkel, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.