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Volumn 8, Issue 9, 2013, Pages

BB0347, from the Lyme Disease Spirochete Borrelia burgdorferi, Is Surface Exposed and Interacts with the CS1 Heparin-Binding Domain of Human Fibronectin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BB0347 PROTEIN; FIBRONECTIN; UNCLASSIFIED DRUG;

EID: 84884682504     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075643     Document Type: Article
Times cited : (29)

References (78)
  • 2
    • 84864812174 scopus 로고    scopus 로고
    • In the clinic. Lyme disease
    • Hu LT, (2012) In the clinic. Lyme disease. Ann Intern Med 157: ITC2-2-ITC2-16.
    • (2012) Ann Intern Med , vol.157 , pp. 2-16
    • Hu, L.T.1
  • 6
    • 79952487225 scopus 로고    scopus 로고
    • The range of Ixodes ricinus and the risk of contracting Lyme borreliosis will increase northwards when the vegetation period becomes longer
    • Jaenson TG, Lindgren E, (2011) The range of Ixodes ricinus and the risk of contracting Lyme borreliosis will increase northwards when the vegetation period becomes longer. Ticks Tick Borne Dis 2: 44-49.
    • (2011) Ticks Tick Borne Dis , vol.2 , pp. 44-49
    • Jaenson, T.G.1    Lindgren, E.2
  • 8
    • 70349293702 scopus 로고    scopus 로고
    • Phylogeography of Borrelia burgdorferi in the eastern United States reflects multiple independent Lyme disease emergence events
    • Hoen AG, Margos G, Bent SJ, Diuk-Wasser MA, Barbour A, et al. (2009) Phylogeography of Borrelia burgdorferi in the eastern United States reflects multiple independent Lyme disease emergence events. Proc Natl Acad Sci U S A 106: 15013-15018.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 15013-15018
    • Hoen, A.G.1    Margos, G.2    Bent, S.J.3    Diuk-Wasser, M.A.4    Barbour, A.5
  • 9
    • 0037265493 scopus 로고    scopus 로고
    • Molecular interaction of Porphyromonas gingivalis with host cells: implication for the microbial pathogenesis of periodontal disease
    • Amano A, (2003) Molecular interaction of Porphyromonas gingivalis with host cells: implication for the microbial pathogenesis of periodontal disease. J Periodontol 74: 90-96.
    • (2003) J Periodontol , vol.74 , pp. 90-96
    • Amano, A.1
  • 11
    • 0032767986 scopus 로고    scopus 로고
    • Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells
    • Joh D, Wann ER, Kreikemeyer B, Speziale P, Höök M, (1999) Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells. Matrix Biol 18: 211-223.
    • (1999) Matrix Biol , vol.18 , pp. 211-223
    • Joh, D.1    Wann, E.R.2    Kreikemeyer, B.3    Speziale, P.4    Höök, M.5
  • 12
    • 77958193852 scopus 로고    scopus 로고
    • Diverse functions of glycosaminoglycans in infectious diseases
    • Aquino RS, Lee ES, Park PW, (2010) Diverse functions of glycosaminoglycans in infectious diseases. Prog Mol Biol Transl Sci 93: 373-394.
    • (2010) Prog Mol Biol Transl Sci , vol.93 , pp. 373-394
    • Aquino, R.S.1    Lee, E.S.2    Park, P.W.3
  • 14
    • 23844515087 scopus 로고    scopus 로고
    • Solving a sticky problem: new genetic approaches to host cell adhesion by the Lyme disease spirochete
    • Coburn J, Fischer JR, Leong JM, (2005) Solving a sticky problem: new genetic approaches to host cell adhesion by the Lyme disease spirochete. Mol Microbiol 57: 1182-1195.
    • (2005) Mol Microbiol , vol.57 , pp. 1182-1195
    • Coburn, J.1    Fischer, J.R.2    Leong, J.M.3
  • 15
    • 48349147505 scopus 로고    scopus 로고
    • Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection
    • Brissette CA, Cooley AE, Burns LH, Riley SP, Verma A, et al. (2008) Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection. Int J Med Microbiol 298Suppl 1: 257-267.
    • (2008) Int J Med Microbiol , vol.298 , pp. 257-267
    • Brissette, C.A.1    Cooley, A.E.2    Burns, L.H.3    Riley, S.P.4    Verma, A.5
  • 16
    • 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
  • 17
    • 77954949043 scopus 로고    scopus 로고
    • A small fibronectin-mimicking protein from bacteria induces cell spreading and focal adhesion formation
    • Tegtmeyer N, Hartig R, Delahay RM, Rohde M, Brandt S, et al. (2010) A small fibronectin-mimicking protein from bacteria induces cell spreading and focal adhesion formation. J Biol Chem 285: 23515-23526.
    • (2010) J Biol Chem , vol.285 , pp. 23515-23526
    • Tegtmeyer, N.1    Hartig, R.2    Delahay, R.M.3    Rohde, M.4    Brandt, S.5
  • 18
    • 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
  • 20
    • 77954716988 scopus 로고    scopus 로고
    • Complement regulator-acquiring surface protein 1 of Borrelia burgdorferi binds to human bone morphogenic protein 2, several extracellular matrix proteins, and plasminogen
    • Hallström T, Haupt K, Kraiczy P, Hortschansky P, Wallich R, et al. (2010) Complement regulator-acquiring surface protein 1 of Borrelia burgdorferi binds to human bone morphogenic protein 2, several extracellular matrix proteins, and plasminogen. J Infect Dis 202: 490-498.
    • (2010) J Infect Dis , vol.202 , pp. 490-498
    • Hallström, T.1    Haupt, K.2    Kraiczy, P.3    Hortschansky, P.4    Wallich, R.5
  • 21
    • 84870254664 scopus 로고    scopus 로고
    • Vascular binding of a pathogen under shear force through mechanistically distinct sequential interactions with host macromolecules
    • Moriarty TJ, Shi M, Lin YP, Ebady R, Zhou H, et al. (2012) Vascular binding of a pathogen under shear force through mechanistically distinct sequential interactions with host macromolecules. Mol Microbiol 86: 1116-1131.
    • (2012) Mol Microbiol , vol.86 , pp. 1116-1131
    • Moriarty, T.J.1    Shi, M.2    Lin, Y.P.3    Ebady, R.4    Zhou, H.5
  • 22
    • 33645092915 scopus 로고    scopus 로고
    • Inactivation of the fibronectin-binding adhesin gene bbk32 significantly attenuates the infectivity potential of Borrelia burgdorferi
    • Seshu J, Esteve-Gassant 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-Gassant, M.D.2    Labandeira-Rey, M.3    Kim, J.H.4    Trzeciakowski, J.P.5
  • 23
    • 80053251616 scopus 로고    scopus 로고
    • Bioluminescent imaging of Borrelia burgdorferi in vivo demonstrates that the fibronectin-binding protein BBK32 is required for optimal infectivity
    • Hyde JA, Weening EH, Chang M, Trzeciakowski JP, Höök M, et al. (2011) Bioluminescent imaging of Borrelia burgdorferi in vivo demonstrates that the fibronectin-binding protein BBK32 is required for optimal infectivity. Mol Microbiol 82: 99-113.
    • (2011) Mol Microbiol , vol.82 , pp. 99-113
    • Hyde, J.A.1    Weening, E.H.2    Chang, M.3    Trzeciakowski, J.P.4    Höök, M.5
  • 24
    • 84864330149 scopus 로고    scopus 로고
    • Comparative molecular analyses of Borrelia burgdorferi sensu stricto strains B31 and N40D10/E9 and determination of their pathogenicity
    • Chan K, Awan M, Barthold SW, Parveen N, (2012) Comparative molecular analyses of Borrelia burgdorferi sensu stricto strains B31 and N40D10/E9 and determination of their pathogenicity. BMC Microbiol 12: 157.
    • (2012) BMC Microbiol , vol.12 , pp. 157
    • Chan, K.1    Awan, M.2    Barthold, S.W.3    Parveen, N.4
  • 25
    • 0032588051 scopus 로고    scopus 로고
    • Fibronectin and alpha5beta1 integrin mediate binding of Pseudomonas aeruginosa to repairing airway epithelium
    • Roger P, Puchelle E, Bajolet-Laudinat O, Tournier JM, Debordeaux C, et al. (1999) Fibronectin and alpha5beta1 integrin mediate binding of Pseudomonas aeruginosa to repairing airway epithelium. Eur Respir J 13: 1301-1309.
    • (1999) Eur Respir J , vol.13 , pp. 1301-1309
    • Roger, P.1    Puchelle, E.2    Bajolet-Laudinat, O.3    Tournier, J.M.4    Debordeaux, C.5
  • 26
    • 31844452509 scopus 로고    scopus 로고
    • Sticky connections: extracellular matrix protein recognition and integrin-mediated cellular invasion by Staphylococcus aureus
    • Hauck CR, Ohlsen K, (2006) Sticky connections: extracellular matrix protein recognition and integrin-mediated cellular invasion by Staphylococcus aureus. Curr Opin Microbiol 9: 5-11.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 5-11
    • Hauck, C.R.1    Ohlsen, K.2
  • 27
    • 79955540132 scopus 로고    scopus 로고
    • Staphylococcus aureus keratinocyte invasion is dependent upon multiple high-affinity fibronectin-binding repeats within FnBPA
    • Edwards AM, Potter U, Meenan NA, Potts JR, Massey RC, (2011) Staphylococcus aureus keratinocyte invasion is dependent upon multiple high-affinity fibronectin-binding repeats within FnBPA. PLoS One 6: e18899.
    • (2011) PLoS One , vol.6
    • Edwards, A.M.1    Potter, U.2    Meenan, N.A.3    Potts, J.R.4    Massey, R.C.5
  • 28
    • 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
  • 29
    • 84867743043 scopus 로고    scopus 로고
    • Acute haematogenous community-acquired methicillin-resistant Staphylococcus aureus osteomyelitis in an adult: Case report and review of literature
    • Dhanoa A, Singh VA, Mansor A, Yusof MY, Lim KT, et al. (2012) Acute haematogenous community-acquired methicillin-resistant Staphylococcus aureus osteomyelitis in an adult: Case report and review of literature. BMC Infect Dis 12: 270.
    • (2012) BMC Infect Dis , vol.12 , pp. 270
    • Dhanoa, A.1    Singh, V.A.2    Mansor, A.3    Yusof, M.Y.4    Lim, K.T.5
  • 30
    • 79959392159 scopus 로고    scopus 로고
    • Role of fibronectin-binding proteins A and B in in vitro cellular infections and in vivo septic infections by Staphylococcus aureus
    • Shinji H, Yosizawa Y, Tajima A, Iwase T, Sugimoto S, et al. (2011) Role of fibronectin-binding proteins A and B in in vitro cellular infections and in vivo septic infections by Staphylococcus aureus. Infect Immun 79: 2215-2223.
    • (2011) Infect Immun , vol.79 , pp. 2215-2223
    • Shinji, H.1    Yosizawa, Y.2    Tajima, A.3    Iwase, T.4    Sugimoto, S.5
  • 31
    • 33748209542 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of gram-positive cocci
    • Schwarz-Linek U, Höök 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    Höök, M.2    Potts, J.R.3
  • 32
    • 0034443264 scopus 로고    scopus 로고
    • Heterologously expressed Staphylococcus aureus fibronectin-binding proteins are sufficient for invasion of host cells
    • Sinha B, Francois P, Que YA, Hussain M, Heilmann C, et al. (2000) Heterologously expressed Staphylococcus aureus fibronectin-binding proteins are sufficient for invasion of host cells. Infect Immun 68: 6871-6878.
    • (2000) Infect Immun , vol.68 , pp. 6871-6878
    • Sinha, B.1    Francois, P.2    Que, Y.A.3    Hussain, M.4    Heilmann, C.5
  • 33
    • 33845490649 scopus 로고    scopus 로고
    • Invasion of human neuronal and glial cells by an infectious strain of Borrelia burgdorferi
    • Livengood JA, Gilmore RD, (2006) Invasion of human neuronal and glial cells by an infectious strain of Borrelia burgdorferi. Microbes Infect 8: 2832-2840.
    • (2006) Microbes Infect , vol.8 , pp. 2832-2840
    • Livengood, J.A.1    Gilmore, R.D.2
  • 34
    • 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
  • 35
    • 79952287105 scopus 로고    scopus 로고
    • Invasion of eukaryotic cells by Borrelia burgdorferi requires β(1) integrins and Src kinase activity
    • Wu J, Weening EH, Faske JB, Höök M, Skare JT, (2011) Invasion of eukaryotic cells by Borrelia burgdorferi requires β(1) integrins and Src kinase activity. Infect Immun 79: 1338-1348.
    • (2011) Infect Immun , vol.79 , pp. 1338-1348
    • Wu, J.1    Weening, E.H.2    Faske, J.B.3    Höök, M.4    Skare, J.T.5
  • 36
    • 8144223362 scopus 로고    scopus 로고
    • Genome-wide transposon mutagenesis of Borrelia burgdorferi for identification of phenotypic mutants
    • Stewart PE, Hoff J, Fischer E, Krum JG, Rosa PA, (2004) Genome-wide transposon mutagenesis of Borrelia burgdorferi for identification of phenotypic mutants. Appl Environ Microbiol 70: 5973-5979.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 5973-5979
    • Stewart, P.E.1    Hoff, J.2    Fischer, E.3    Krum, J.G.4    Rosa, P.A.5
  • 37
    • 79952591597 scopus 로고    scopus 로고
    • Relationship between immunity to Borrelia burgdorferi outer-surface protein A (OspA) and Lyme arthritis
    • Steere AC, Drouin EE, Glickstein LJ, (2011) Relationship between immunity to Borrelia burgdorferi outer-surface protein A (OspA) and Lyme arthritis. Clin Infect Dis 52Suppl 3: s259-s265.
    • (2011) Clin Infect Dis , vol.52
    • Steere, A.C.1    Drouin, E.E.2    Glickstein, L.J.3
  • 38
    • 0031470826 scopus 로고    scopus 로고
    • Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi
    • Fraser CM, Casjens S, Huang WM, Sutton GG, Clayton R, et al. (1997) Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390: 580-586.
    • (1997) Nature , vol.390 , pp. 580-586
    • Fraser, C.M.1    Casjens, S.2    Huang, W.M.3    Sutton, G.G.4    Clayton, R.5
  • 39
    • 0033975239 scopus 로고    scopus 로고
    • A bacterial genome in flux: the twelve linear and nine circular extrachromosomal DNAs in an infectious isolate of the Lyme disease spirochete Borrelia burgdorferi
    • Casjens S, Palmer N, Van Vugt R, Mun Huang W, Stevenson B, et al. (2002) A bacterial genome in flux: the twelve linear and nine circular extrachromosomal DNAs in an infectious isolate of the Lyme disease spirochete Borrelia burgdorferi. Mol Microbiol 35: 490-516.
    • (2002) Mol Microbiol , vol.35 , pp. 490-516
    • Casjens, S.1    Palmer, N.2    Van Vugt, R.3    Mun Huang, W.4    Stevenson, B.5
  • 40
    • 0021671855 scopus 로고
    • Isolation and cultivation of Lyme disease spirochetes
    • Barbour AG, (1984) Isolation and cultivation of Lyme disease spirochetes. The Yale J Biol Med 57: 521.
    • (1984) The Yale J Biol Med , vol.57 , pp. 521
    • Barbour, A.G.1
  • 41
    • 79959747151 scopus 로고    scopus 로고
    • Multiplex PCR as a tool for validating plasmid content of Borrelia burgdorferi
    • Bunikis I, Kutschan-Bunikis S, Bonde M, Bergström S, (2011) Multiplex PCR as a tool for validating plasmid content of Borrelia burgdorferi. J Microbiol Methods 86: 243-247.
    • (2011) J Microbiol Methods , vol.86 , pp. 243-247
    • Bunikis, I.1    Kutschan-Bunikis, S.2    Bonde, M.3    Bergström, S.4
  • 42
    • 84856866886 scopus 로고    scopus 로고
    • Fibronectin binding to the Treponema pallidum adhesin protein fragment rTp0483 on functionalized self-assembled monolayers
    • Dickerson MT, Abney MB, Cameron CE, Knecht M, Bachas LG, et al. (2012) Fibronectin binding to the Treponema pallidum adhesin protein fragment rTp0483 on functionalized self-assembled monolayers. Bioconjug Chem 23: 184-195.
    • (2012) Bioconjug Chem , vol.23 , pp. 184-195
    • Dickerson, M.T.1    Abney, M.B.2    Cameron, C.E.3    Knecht, M.4    Bachas, L.G.5
  • 43
    • 84891457308 scopus 로고    scopus 로고
    • Evaluation of RevA, a fibronectin-binding protein of Borrelia burgdorferi, as a potential vaccine candidate for Lyme disease
    • Floden AM, Gonzalez T, Gaultney RA, Brissette CA, (2013) Evaluation of RevA, a fibronectin-binding protein of Borrelia burgdorferi, as a potential vaccine candidate for Lyme disease. Clin Vaccine Immunol 20: 892-899.
    • (2013) Clin Vaccine Immunol , vol.20 , pp. 892-899
    • Floden, A.M.1    Gonzalez, T.2    Gaultney, R.A.3    Brissette, C.A.4
  • 44
    • 84866316666 scopus 로고    scopus 로고
    • Borrelia burgdorferi cp32 BpaB modulates expression of the prophage NucP nuclease and SsbP single-stranded DNA-binding protein
    • Chenail AM, Jutras BL, Adams CA, Burns LH, Bowman A, et al. (2012) Borrelia burgdorferi cp32 BpaB modulates expression of the prophage NucP nuclease and SsbP single-stranded DNA-binding protein. J Bacteriol 194: 4570-4578.
    • (2012) J Bacteriol , vol.194 , pp. 4570-4578
    • Chenail, A.M.1    Jutras, B.L.2    Adams, C.A.3    Burns, L.H.4    Bowman, A.5
  • 45
    • 84868292505 scopus 로고    scopus 로고
    • Whole genome sequencing of the fish pathogen Francisella noatunensis subsp. orientalis Toba04 gives novel insights into Francisella evolution and pathogenicity
    • Sridhar S, Sharma A, Kongshaug H, Nilsen F, Jonassen I, (2012) Whole genome sequencing of the fish pathogen Francisella noatunensis subsp. orientalis Toba04 gives novel insights into Francisella evolution and pathogenicity. BMC Genomics 13: 598.
    • (2012) BMC Genomics , vol.13 , pp. 598
    • Sridhar, S.1    Sharma, A.2    Kongshaug, H.3    Nilsen, F.4    Jonassen, I.5
  • 46
    • 84867114038 scopus 로고    scopus 로고
    • Antigen variability in Anaplasma phagocytophilum during chronic infection of a reservoir host
    • Rejmanek D, Foley P, Barbet A, Foley J, (2012) Antigen variability in Anaplasma phagocytophilum during chronic infection of a reservoir host. Microbiol 158: 2632-2641.
    • (2012) Microbiol , vol.158 , pp. 2632-2641
    • Rejmanek, D.1    Foley, P.2    Barbet, A.3    Foley, J.4
  • 47
    • 84868670393 scopus 로고    scopus 로고
    • Genome-derived insights into the biology of the hepatotoxic bloom-forming cyanobacterium Anabaena sp. strain 90
    • Wang H, Sivonen K, Rouhiainen L, Fewer DP, Lyra C, et al. (2012) Genome-derived insights into the biology of the hepatotoxic bloom-forming cyanobacterium Anabaena sp. strain 90. BMC Genomics 13: 613.
    • (2012) BMC Genomics , vol.13 , pp. 613
    • Wang, H.1    Sivonen, K.2    Rouhiainen, L.3    Fewer, D.P.4    Lyra, C.5
  • 48
    • 84865808846 scopus 로고    scopus 로고
    • Reduced mRNA secondary-structure stability near the start codon indicates functional genes in prokaryotes
    • Keller TE, Mis SD, Jia KE, Wilke CO, (2012) Reduced mRNA secondary-structure stability near the start codon indicates functional genes in prokaryotes. Genome Biol Evol 4: 80-88.
    • (2012) Genome Biol Evol , vol.4 , pp. 80-88
    • Keller, T.E.1    Mis, S.D.2    Jia, K.E.3    Wilke, C.O.4
  • 49
    • 21344470130 scopus 로고    scopus 로고
    • Inhibitory effect of fucoidan on the adhesion of adenocarcinoma cells to fibronectin
    • Liu JM, Bignon J, Haroun-Bouhedja F, Bittoun P, Vassy J, et al. (2005) Inhibitory effect of fucoidan on the adhesion of adenocarcinoma cells to fibronectin. Anticancer Res 25: 2129-2133.
    • (2005) Anticancer Res , vol.25 , pp. 2129-2133
    • Liu, J.M.1    Bignon, J.2    Haroun-Bouhedja, F.3    Bittoun, P.4    Vassy, J.5
  • 50
    • 1142287523 scopus 로고    scopus 로고
    • Adherence of Actinobacillus pleuropneumoniae serotype 1 to swine buccal epithelial cells involves fibronectin
    • Hamer-Barrera R, Godínez D, Enríquez VI, Vaca-Pacheco S, Martinez-Zúñiga R, et al. (2004) Adherence of Actinobacillus pleuropneumoniae serotype 1 to swine buccal epithelial cells involves fibronectin. Can J Vet Res 68: 33-41.
    • (2004) Can J Vet Res , vol.68 , pp. 33-41
    • Hamer-Barrera, R.1    Godínez, D.2    Enríquez, V.I.3    Vaca-Pacheco, S.4    Martinez-Zúñiga, R.5
  • 51
    • 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
  • 52
    • 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, Bäumler 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    Bäumler, A.J.4
  • 54
    • 80555140065 scopus 로고    scopus 로고
    • Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein
    • Floden AM, Watt JA, Brissette CA, (2011) Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein. PLoS One 6: e27502.
    • (2011) PLoS One , vol.6
    • Floden, A.M.1    Watt, J.A.2    Brissette, C.A.3
  • 55
    • 79960929092 scopus 로고    scopus 로고
    • Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin
    • Boone TJ, Burnham CA, Tyrrell GJ, (2011) Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin. Microb Pathog 51: 255-261.
    • (2011) Microb Pathog , vol.51 , pp. 255-261
    • Boone, T.J.1    Burnham, C.A.2    Tyrrell, G.J.3
  • 56
    • 77949420679 scopus 로고    scopus 로고
    • Methods of identifying membrane proteins in spirochetes
    • Unit12C.2
    • Carroll JA, (2010) Methods of identifying membrane proteins in spirochetes. Curr Protoc Microbiol Chapter 12: Unit12C.2.
    • (2010) Curr Protoc Microbiol Chapter , vol.12
    • Carroll, J.A.1
  • 57
    • 77953952245 scopus 로고    scopus 로고
    • Role of the surface lipoprotein BBA07 in the enzootic cycle of Borrelia burgdorferi
    • Xu H, He M, He JJ, Yang XF, (2010) Role of the surface lipoprotein BBA07 in the enzootic cycle of Borrelia burgdorferi. Infect Immun 78: 2910-2918.
    • (2010) Infect Immun , vol.78 , pp. 2910-2918
    • Xu, H.1    He, M.2    He, J.J.3    Yang, X.F.4
  • 58
    • 84863256882 scopus 로고    scopus 로고
    • A surface enolase participates in Borrelia burgdorferi-plasminogen interaction and contributes to pathogen survival within feeding ticks
    • Nogueira SV, Smith AA, Qin JH, Pal U, (2012) A surface enolase participates in Borrelia burgdorferi-plasminogen interaction and contributes to pathogen survival within feeding ticks. Infect Immun 80: 82-90.
    • (2012) Infect Immun , vol.80 , pp. 82-90
    • Nogueira, S.V.1    Smith, A.A.2    Qin, J.H.3    Pal, U.4
  • 59
    • 0029855068 scopus 로고    scopus 로고
    • Structural analysis of the Leptospiraceae and Borrelia burgdorferi by high-voltage electron microscopy
    • Goldstein SF, Buttle KF, Charon NW, (1996) Structural analysis of the Leptospiraceae and Borrelia burgdorferi by high-voltage electron microscopy. J Bacteriol 178: 6539-6545.
    • (1996) J Bacteriol , vol.178 , pp. 6539-6545
    • Goldstein, S.F.1    Buttle, K.F.2    Charon, N.W.3
  • 60
    • 0034718538 scopus 로고    scopus 로고
    • Borrelia burgdorferi periplasmic flagella have both skeletal and motility functions
    • Motaleb MA, Corum L, Bono JL, Elias AF, Rosa P, et al. (2000) Borrelia burgdorferi periplasmic flagella have both skeletal and motility functions. Proc Natl Acad Sci U S A 97: 10899-10904.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10899-10904
    • Motaleb, M.A.1    Corum, L.2    Bono, J.L.3    Elias, A.F.4    Rosa, P.5
  • 61
    • 84860847495 scopus 로고    scopus 로고
    • OspC is potent plasminogen receptor on surface of Borrelia burgdorferi
    • Önder Ö, Humphrey PT, McOmber B, Korobova F, Francella N, et al. (2012) OspC is potent plasminogen receptor on surface of Borrelia burgdorferi. J Biol Chem 287: 16860-16868.
    • (2012) J Biol Chem , vol.287 , pp. 16860-16868
    • Önder, Ö.1    Humphrey, P.T.2    McOmber, B.3    Korobova, F.4    Francella, N.5
  • 62
    • 0027309262 scopus 로고
    • Immunological and molecular polymorphisms of OspC, an immunodominant major outer surface protein of Borrelia burgdorferi
    • Wilske B, Preac-Mursic V, Jauris S, Hofmann A, Pradel I, et al. (1993) Immunological and molecular polymorphisms of OspC, an immunodominant major outer surface protein of Borrelia burgdorferi. Infect Immun 61: 2182-2191.
    • (1993) Infect Immun , vol.61 , pp. 2182-2191
    • Wilske, B.1    Preac-Mursic, V.2    Jauris, S.3    Hofmann, A.4    Pradel, I.5
  • 63
    • 80053599548 scopus 로고    scopus 로고
    • Specificity and role of the Borrelia burgdorferi Tap protease in outer membrane protein processing
    • Kumru OS, Bunikis I, Sorokina I, Bergström S, Zückert WR, (2011) Specificity and role of the Borrelia burgdorferi Tap protease in outer membrane protein processing. J Bacteriol 193: 5759-5765.
    • (2011) J Bacteriol , vol.193 , pp. 5759-5765
    • Kumru, O.S.1    Bunikis, I.2    Sorokina, I.3    Bergström, S.4    Zückert, W.R.5
  • 64
    • 67650694036 scopus 로고    scopus 로고
    • A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans
    • Pinne M, Haake DA, (2009) A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans. PLoS One 4: e6071.
    • (2009) PLoS One , vol.4
    • Pinne, M.1    Haake, D.A.2
  • 65
    • 84865775747 scopus 로고    scopus 로고
    • The PavA-like fibronectin-binding protein of Enterococcus faecalis, EfbA, is important for virulence in a mouse model of ascending urinary tract infection
    • Torelli R, Serror P, Bugli F, Sterbini FP, Florio AR, et al. (2012) The PavA-like fibronectin-binding protein of Enterococcus faecalis, EfbA, is important for virulence in a mouse model of ascending urinary tract infection. J Infect Disease 206: 952-960.
    • (2012) J Infect Disease , vol.206 , pp. 952-960
    • Torelli, R.1    Serror, P.2    Bugli, F.3    Sterbini, F.P.4    Florio, A.R.5
  • 66
    • 77949701439 scopus 로고    scopus 로고
    • Analysis of the dbpBA upstream regulatory region controlled by RpoS in Borrelia burgdorferi
    • Ouyang Z, Haq S, Norgard MV, (2010) Analysis of the dbpBA upstream regulatory region controlled by RpoS in Borrelia burgdorferi. J Bacteriol 192: 1965-1974.
    • (2010) J Bacteriol , vol.192 , pp. 1965-1974
    • Ouyang, Z.1    Haq, S.2    Norgard, M.V.3
  • 67
    • 0034056597 scopus 로고    scopus 로고
    • Temperature-regulated expression of bacterial virulence genes
    • Konkel ME, Tilly K, (2000) Temperature-regulated expression of bacterial virulence genes. Microbes infect 2: 157-166.
    • (2000) Microbes Infect , vol.2 , pp. 157-166
    • Konkel, M.E.1    Tilly, K.2
  • 69
    • 84875078664 scopus 로고    scopus 로고
    • A comparative analysis of the properties of regulated promoter systems commonly used for recombinant gene expression in Escherichia coli
    • Balzer S, Kucharova V, Megerle J, Lale R, Brautaset T, et al. (2013) A comparative analysis of the properties of regulated promoter systems commonly used for recombinant gene expression in Escherichia coli. Microb Cell Fact 12: 26.
    • (2013) Microb Cell Fact , vol.12 , pp. 26
    • Balzer, S.1    Kucharova, V.2    Megerle, J.3    Lale, R.4    Brautaset, T.5
  • 70
    • 0037188523 scopus 로고    scopus 로고
    • Long-term and homogeneous regulation of the Escherichia coli araBAD promoter by use of a lactose transporter of relaxed specificity
    • Morgan-Kiss RM, Wadler C, Cronan JE, (2002) Long-term and homogeneous regulation of the Escherichia coli araBAD promoter by use of a lactose transporter of relaxed specificity. Proc Nat Acad Sci USA 99: 7373-7377.
    • (2002) Proc Nat Acad Sci USA , vol.99 , pp. 7373-7377
    • Morgan-Kiss, R.M.1    Wadler, C.2    Cronan, J.E.3
  • 71
    • 0343593690 scopus 로고    scopus 로고
    • Inhibition of Borrelia burgdorferi migration from the midgut to the salivary glands following feeding by ticks on OspC-immunized mice
    • Gilmore RD, Piesman J, (2000) Inhibition of Borrelia burgdorferi migration from the midgut to the salivary glands following feeding by ticks on OspC-immunized mice. Infect Immun 68: 411-414.
    • (2000) Infect Immun , vol.68 , pp. 411-414
    • Gilmore, R.D.1    Piesman, J.2
  • 72
    • 38049107588 scopus 로고    scopus 로고
    • Borrelia burgdorferi BBB07 interaction with integrin alpha3beta1 stimulates production of pro-inflammatory mediators in primary human chondrocytes
    • Behera AK, Durand E, Cugini C, Antonara S, Bourassa L, et al. (2008) Borrelia burgdorferi BBB07 interaction with integrin alpha3beta1 stimulates production of pro-inflammatory mediators in primary human chondrocytes. Cell Microbiol 10: 320-331.
    • (2008) Cell Microbiol , vol.10 , pp. 320-331
    • Behera, A.K.1    Durand, E.2    Cugini, C.3    Antonara, S.4    Bourassa, L.5
  • 73
    • 33748328139 scopus 로고    scopus 로고
    • The matrix reorganized: extracellular matrix remodeling and integrin signaling
    • Larsen M, Artym VV, Green JA, Yamada KM, (2006) The matrix reorganized: extracellular matrix remodeling and integrin signaling. Curr Opin Cell Biol 18: 463-471.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 463-471
    • Larsen, M.1    Artym, V.V.2    Green, J.A.3    Yamada, K.M.4
  • 74
    • 33646384575 scopus 로고    scopus 로고
    • Bartonella henselae Pap31, an extracellular matrix adhesin, binds the fibronectin repeat III13 module
    • Dabo SM, Confer AW, Anderson BE, Gupta S, (2006) Bartonella henselae Pap31, an extracellular matrix adhesin, binds the fibronectin repeat III13 module. Infect Immun 74: 2513-2521.
    • (2006) Infect Immun , vol.74 , pp. 2513-2521
    • Dabo, S.M.1    Confer, A.W.2    Anderson, B.E.3    Gupta, S.4
  • 75
    • 84870363959 scopus 로고    scopus 로고
    • Immunogenic characterization of outer membrane porins OmpC and OmpF of porcine extraintestinal pathogenic Escherichia coli
    • Liu C, Chen Z, Tan C, Liu W, Xu Z, et al. (2012) Immunogenic characterization of outer membrane porins OmpC and OmpF of porcine extraintestinal pathogenic Escherichia coli. FEMS Microbiol Lett 337: 104-111.
    • (2012) FEMS Microbiol Lett , vol.337 , pp. 104-111
    • Liu, C.1    Chen, Z.2    Tan, C.3    Liu, W.4    Xu, Z.5
  • 76
    • 84862336998 scopus 로고    scopus 로고
    • Immunogenicity and protective potential of a bacterially expressed recombinant dihydrolipoamide succinyltransferase (rE2o) of Brucella abortus in BALB/c mice
    • Verma SK, Jain S, Kumar S, (2012) Immunogenicity and protective potential of a bacterially expressed recombinant dihydrolipoamide succinyltransferase (rE2o) of Brucella abortus in BALB/c mice. World J Microbiol Biotechnol 28: 2487-2495.
    • (2012) World J Microbiol Biotechnol , vol.28 , pp. 2487-2495
    • Verma, S.K.1    Jain, S.2    Kumar, S.3
  • 77
    • 84856042853 scopus 로고    scopus 로고
    • Serum antibodies to whole-cell and recombinant antigens of Borrelia burgdorferi in cottontail rabbits
    • Magnarelli LA, Norris SJ, Fikrig E, (2012) Serum antibodies to whole-cell and recombinant antigens of Borrelia burgdorferi in cottontail rabbits. J Wildl Dis 48: 12-20.
    • (2012) J Wildl Dis , vol.48 , pp. 12-20
    • Magnarelli, L.A.1    Norris, S.J.2    Fikrig, E.3
  • 78
    • 84876049861 scopus 로고    scopus 로고
    • Serum antibodies to Borrelia burgdorferi, Anaplasma phagocytophilum, and Babesia microti in recaptured white-footed mice
    • Magnarelli LA, Williams SC, Norris SJ, Fikrig E, (2013) Serum antibodies to Borrelia burgdorferi, Anaplasma phagocytophilum, and Babesia microti in recaptured white-footed mice. J Wildl Dis 49: 294-302.
    • (2013) J Wildl Dis , vol.49 , pp. 294-302
    • Magnarelli, L.A.1    Williams, S.C.2    Norris, S.J.3    Fikrig, E.4


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