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Volumn 4, Issue 4, 2009, Pages

A novel fibronectin binding motif in MSCRAMMs targets F3 modules

Author keywords

[No Author keywords available]

Indexed keywords

ANASTELLIN; BACTERIAL PROTEIN; FIBRONECTIN; FIBRONECTIN F3; LIPOPROTEIN; MICROBIAL SURFACE COMPONENT RECOGNIZING ADHESIVE MATRIX MOLECULE; PROTEIN BBK32; RECOMBINANT PROTEIN; RECOMBINANT PROTEIN BBK32; SUPERFIBRONECTIN; THERMOLYSIN; UNCLASSIFIED DRUG; ADHESIN; P35 ANTIGEN, BORRELIA; PEPTIDE FRAGMENT; VIRULENCE FACTOR; VIRUS RECEPTOR;

EID: 65549112108     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005412     Document Type: Article
Times cited : (34)

References (42)
  • 2
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules
    • Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM (1997) A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. J Mol Biol 270: 763-770.
    • (1997) J Mol Biol , vol.270 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 3
    • 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
  • 4
    • 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 Biology 24: 389-399.
    • (2005) Matrix Biology , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 5
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis
    • Pankov R, Cukierman E, Katz BZ, Matsumoto K, Lin DC, et al. (2000) Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. J Cell Biol 148: 1075-1090.
    • (2000) J Cell Biol , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5
  • 6
    • 0034092910 scopus 로고    scopus 로고
    • A novel RGD-independent fibronectin assembly pathway initiated by alpha4beta1 integrin binding to the alternatively spliced V region
    • Sechler JL, Cumiskey AM, Gazzola DM, Schwarzbauer JE (2000) A novel RGD-independent fibronectin assembly pathway initiated by alpha4beta1 integrin binding to the alternatively spliced V region. J Cell Sci 113(Pt 8): 1491-1498.
    • (2000) J Cell Sci , vol.113 , Issue.PART 8 , pp. 1491-1498
    • Sechler, J.L.1    Cumiskey, A.M.2    Gazzola, D.M.3    Schwarzbauer, J.E.4
  • 7
    • 34249067404 scopus 로고    scopus 로고
    • Interdomain association in fibronectin: Insight into cryptic sites and fibrillogenesis
    • Vakonakis I, Staunton D, Rooney LM, Campbell ID (2007) Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis. Embo J 26: 2575-2583.
    • (2007) Embo J , vol.26 , pp. 2575-2583
    • Vakonakis, I.1    Staunton, D.2    Rooney, L.M.3    Campbell, I.D.4
  • 8
    • 0004133195 scopus 로고
    • San Diego: Academic Press, Inc
    • Mosher DF (1989) Fibronectin. San Diego: Academic Press, Inc.
    • (1989) Fibronectin
    • Mosher, D.F.1
  • 9
    • 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
  • 10
    • 0042235309 scopus 로고    scopus 로고
    • Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors
    • Briknarova K, Akerman ME, 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, M.E.2    Hoyt, D.W.3    Ruoslahti, E.4    Ely, K.R.5
  • 11
    • 28244461501 scopus 로고    scopus 로고
    • Domain unfolding plays a role in super-fibronectin formation
    • Ohashi T, Erickson HP (2005) Domain unfolding plays a role in super-fibronectin formation. J Biol Chem 280: 39143-39151.
    • (2005) J Biol Chem , vol.280 , pp. 39143-39151
    • Ohashi, T.1    Erickson, H.P.2
  • 12
    • 13844315323 scopus 로고    scopus 로고
    • Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature
    • Akerman ME, Pilch J, Peters D, Ruoslahti E (2005) Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature. Proc Natl Acad Sci U S A 102: 2040-2045.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2040-2045
    • Akerman, M.E.1    Pilch, J.2    Peters, D.3    Ruoslahti, E.4
  • 13
    • 0035895247 scopus 로고    scopus 로고
    • A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis
    • Yi M, Ruoslahti E (2001) A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis. Proc Natl Acad Sci U S A 98: 620-624.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 620-624
    • Yi, M.1    Ruoslahti, E.2
  • 14
    • 11244261710 scopus 로고    scopus 로고
    • Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells
    • Ambesi A, Klein RM, Pumiglia KM, McKeown-Longo PJ (2005) Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells. Cancer Res 65: 148-156.
    • (2005) Cancer Res , vol.65 , pp. 148-156
    • Ambesi, A.1    Klein, R.M.2    Pumiglia, K.M.3    McKeown-Longo, P.J.4
  • 15
    • 1942501147 scopus 로고    scopus 로고
    • The ShdA adhesin binds to the cationic cradle of the fibronectin 13FnIII repeat module: Evidence for molecular mimicry of heparin binding
    • Kingsley RA, Keestra AM, de Zoete MR, Baumler AJ (2004) The ShdA adhesin binds to the cationic cradle of the fibronectin 13FnIII repeat module: evidence for molecular mimicry of heparin binding. Mol Microbiol 52: 345-355.
    • (2004) Mol Microbiol , vol.52 , pp. 345-355
    • Kingsley, R.A.1    Keestra, A.M.2    de Zoete, M.R.3    Baumler, A.J.4
  • 16
    • 0031769859 scopus 로고    scopus 로고
    • Identification of a 47 kDa fibronectin-binding protein expressed by Borrelia burgdorferi isolate B31
    • Probert WS, Johnson BJ (1998) Identification of a 47 kDa fibronectin-binding protein expressed by Borrelia burgdorferi isolate B31. Mol Microbiol 30: 1003-1015.
    • (1998) Mol Microbiol , vol.30 , pp. 1003-1015
    • Probert, W.S.1    Johnson, B.J.2
  • 17
    • 0036209982 scopus 로고    scopus 로고
    • Recombinant BBK32 protein in serodiagnosis of early and late Lyme borreliosis
    • Heikkila T, Seppala I, Saxen H, Panelius J, Peltomaa M, et al. (2002) Recombinant BBK32 protein in serodiagnosis of early and late Lyme borreliosis. J Clin Microbiol 40: 1174-1180.
    • (2002) J Clin Microbiol , vol.40 , pp. 1174-1180
    • Heikkila, T.1    Seppala, I.2    Saxen, H.3    Panelius, J.4    Peltomaa, M.5
  • 18
    • 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 3rd, 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 3rd, S.R.4    Flavell, R.A.5
  • 19
    • 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 BJ, Potts JR, et al. (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.4    Potts, J.R.5
  • 20
    • 21444441457 scopus 로고    scopus 로고
    • Borrelia burgdorferi binds fibronectin through a tandem beta-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci, and spirochetes
    • Raibaud S, Schwarz-Linek U, Kim JH, Jenkins HT, Baines ER, et al. (2005) Borrelia burgdorferi binds fibronectin through a tandem beta-zipper, a common mechanism of fibronectin binding in staphylococci, streptococci, and spirochetes. J Biol Chem 280: 18803-18809.
    • (2005) J Biol Chem , vol.280 , pp. 18803-18809
    • Raibaud, S.1    Schwarz-Linek, U.2    Kim, J.H.3    Jenkins, H.T.4    Baines, E.R.5
  • 21
    • 0031036225 scopus 로고    scopus 로고
    • Cryptic self-association sites in type III modules of fibronectin
    • Ingham KC, Brew SA, Huff S, Litvinovich SV (1997) Cryptic self-association sites in type III modules of fibronectin. J Biol Chem 272: 1718-1724.
    • (1997) J Biol Chem , vol.272 , pp. 1718-1724
    • Ingham, K.C.1    Brew, S.A.2    Huff, S.3    Litvinovich, S.V.4
  • 22
    • 0033580939 scopus 로고    scopus 로고
    • Identification of two amino acids within the EIIIA (ED-A) segment of fibronectin constituting the epitope for two function-blocking monoclonal antibodies
    • Liao YF, Wieder KG, Classen JM, Van De Water L (1999) Identification of two amino acids within the EIIIA (ED-A) segment of fibronectin constituting the epitope for two function-blocking monoclonal antibodies. J Biol Chem 274: 17876-17884.
    • (1999) J Biol Chem , vol.274 , pp. 17876-17884
    • Liao, Y.F.1    Wieder, K.G.2    Classen, J.M.3    Van De Water, L.4
  • 23
    • 0023650942 scopus 로고
    • Localization of the cellular-fibronectin-specific epitope recognized by the monoclonal antibody IST-9 using fusion proteins expressed in E. coli
    • Carnemolla B, Borsi L, Zardi L, Owens RJ, Baralle FE (1987) Localization of the cellular-fibronectin-specific epitope recognized by the monoclonal antibody IST-9 using fusion proteins expressed in E. coli. FEBS Lett 215: 269-273.
    • (1987) FEBS Lett , vol.215 , pp. 269-273
    • Carnemolla, B.1    Borsi, L.2    Zardi, L.3    Owens, R.J.4    Baralle, F.E.5
  • 24
    • 0345328658 scopus 로고    scopus 로고
    • Stimulation of extracellular matrix remodeling by the first type III repeat in fibronectin
    • Klein RM, Zheng M, Ambesi A, Van De Water L, McKeown-Longo PJ (2003) Stimulation of extracellular matrix remodeling by the first type III repeat in fibronectin. J Cell Sci 116: 4663-4674.
    • (2003) J Cell Sci , vol.116 , pp. 4663-4674
    • Klein, R.M.1    Zheng, M.2    Ambesi, A.3    Van De Water, L.4    McKeown-Longo, P.J.5
  • 25
    • 0029907050 scopus 로고    scopus 로고
    • A polymeric form of fibronectin has antimetastatic effects against multiple tumor types
    • Pasqualini R, Bourdoulous S, Koivunen E, Woods VL Jr, Ruoslahti E (1996) A polymeric form of fibronectin has antimetastatic effects against multiple tumor types. Nat Med 2: 1197-1203.
    • (1996) Nat Med , vol.2 , pp. 1197-1203
    • Pasqualini, R.1    Bourdoulous, S.2    Koivunen, E.3    Woods Jr, V.L.4    Ruoslahti, E.5
  • 26
    • 0029986634 scopus 로고    scopus 로고
    • A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix
    • Ozeri V, Tovi A, Burstein I, Natanson-Yaron S, Caparon MG, et al. (1996) A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix. Embo J 15: 989-998.
    • (1996) Embo J , vol.15 , pp. 989-998
    • Ozeri, V.1    Tovi, A.2    Burstein, I.3    Natanson-Yaron, S.4    Caparon, M.G.5
  • 27
    • 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, et al. (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
  • 28
    • 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
  • 29
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SFMTL, Schäffer AA, Zhang J, Zhang Z, Miller W, D.J. L (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • SFMTL, A.1    Schäffer, A.A.2    Zhang, J.3    Zhang, Z.4    Miller, W.D.J.L.5
  • 30
    • 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 C, Schrenzel J, Peters G, et al. (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, C.3    Schrenzel, J.4    Peters, G.5
  • 31
    • 0026706763 scopus 로고
    • Fibronectin-binding protein of Streptococcus pyogenes: Sequence of the binding domain involved in adherence of streptococci to epithelial cells
    • Talay SR, Valentin-Weigand P, Jerlstrom PG, Timmis KN, Chhatwal GS (1992) Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun 60: 3837-3844.
    • (1992) Infect Immun , vol.60 , pp. 3837-3844
    • Talay, S.R.1    Valentin-Weigand, P.2    Jerlstrom, P.G.3    Timmis, K.N.4    Chhatwal, G.S.5
  • 32
    • 0027308871 scopus 로고
    • Fibronectin binding site in type I collagen regulates fibronectin fibril formation
    • Dzamba BJ, Wu H, Jaenisch R, Peters DM (1993) Fibronectin binding site in type I collagen regulates fibronectin fibril formation. J Cell Biol 121: 1165-1172.
    • (1993) J Cell Biol , vol.121 , pp. 1165-1172
    • Dzamba, B.J.1    Wu, H.2    Jaenisch, R.3    Peters, D.M.4
  • 33
    • 55449126064 scopus 로고    scopus 로고
    • Norman MU, Moriarty TJ, Dresser AR, Millen B, Kubes P, et al. (2008) Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host. PLoS Pathog 4: e1000169.
    • Norman MU, Moriarty TJ, Dresser AR, Millen B, Kubes P, et al. (2008) Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host. PLoS Pathog 4: e1000169.
  • 34
    • 0024522287 scopus 로고
    • Penetration of endothelial cell monolayers by Borrelia burgdorferi
    • Comstock LE, Thomas DD (1989) Penetration of endothelial cell monolayers by Borrelia burgdorferi. Infect Immun 57: 1626-1628.
    • (1989) Infect Immun , vol.57 , pp. 1626-1628
    • Comstock, L.E.1    Thomas, D.D.2
  • 35
    • 0026112418 scopus 로고
    • Characterization of Borrelia burgdorferi invasion of cultured endothelial cells
    • Comstock LE, Thomas DD (1991) Characterization of Borrelia burgdorferi invasion of cultured endothelial cells. Microb Pathog 10: 137-148.
    • (1991) Microb Pathog , vol.10 , pp. 137-148
    • Comstock, L.E.1    Thomas, D.D.2
  • 36
    • 0026030704 scopus 로고
    • Intracellular localization of Borrelia burgdorferi within human endothelial cells
    • Ma Y, Sturrock A, Weis JJ (1991) Intracellular localization of Borrelia burgdorferi within human endothelial cells. Infect Immun 59: 671-678.
    • (1991) Infect Immun , vol.59 , pp. 671-678
    • Ma, Y.1    Sturrock, A.2    Weis, J.J.3
  • 38
    • 0024542170 scopus 로고
    • Interaction of Lyme disease spirochetes with cultured eucaryotic cells
    • Thomas DD, Comstock LE (1989) Interaction of Lyme disease spirochetes with cultured eucaryotic cells. Infect Immun 57: 1324-1326.
    • (1989) Infect Immun , vol.57 , pp. 1324-1326
    • Thomas, D.D.1    Comstock, L.E.2
  • 39
    • 33645092915 scopus 로고    scopus 로고
    • Inactivation of the fibronectin-binding adhesin gene bbk32 significantly attenuates the infectivity potential of Borrelia burgdorferi
    • Seshu J, Esteve-Gassent MD, Labandeira-Rey M, Kim JH, Trzeciakowski JP, et al. (2006) Inactivation of the fibronectin-binding adhesin 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    Labandeira-Rey, M.3    Kim, J.H.4    Trzeciakowski, J.P.5
  • 40
    • 0037177894 scopus 로고    scopus 로고
    • The EIIIA segment of fibronectin is a ligand for integrins alpha 9beta 1 and alpha 4beta 1 providing a novel mechanism for regulating cell adhesion by alternative splicing
    • Liao YF, Gotwals PJ, Koteliansky VE, Sheppard D, Van De Water L (2002) The EIIIA segment of fibronectin is a ligand for integrins alpha 9beta 1 and alpha 4beta 1 providing a novel mechanism for regulating cell adhesion by alternative splicing. J Biol Chem 277: 14467-14474.
    • (2002) J Biol Chem , vol.277 , pp. 14467-14474
    • Liao, Y.F.1    Gotwals, P.J.2    Koteliansky, V.E.3    Sheppard, D.4    Van De Water, L.5
  • 41
    • 0027436402 scopus 로고
    • Fibronectin receptors from Streptococcus dysgalactiae and Staphylococcus aureus. Involvement of conserved residues in ligand binding
    • McGavin MJ, Gurusiddappa S, Lindgren PE, Lindberg M, Raucci G, et al. (1993) Fibronectin receptors from Streptococcus dysgalactiae and Staphylococcus aureus. Involvement of conserved residues in ligand binding. J Biol Chem 268: 23946-23953.
    • (1993) J Biol Chem , vol.268 , pp. 23946-23953
    • McGavin, M.J.1    Gurusiddappa, S.2    Lindgren, P.E.3    Lindberg, M.4    Raucci, G.5
  • 42
    • 0018582608 scopus 로고
    • Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions
    • Vuento M, Vaheri A (1979) Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions. Biochem J 183: 331-337.
    • (1979) Biochem J , vol.183 , pp. 331-337
    • Vuento, M.1    Vaheri, A.2


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