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Infection and Immunity
Volumn 82, Issue 3, 2014, Pages 1007-1016
BsaB, a novel adherence factor of group B Streptococcus
Author keywords

[No Author keywords available]
Indexed keywords

ADHESINS, BACTERIAL; BACTERIAL PROTEINS; BIOFILMS; CELL LINE; EPITHELIAL CELLS; EXTRACELLULAR MATRIX; FIBRONECTINS; HUMANS; LACTOCOCCUS LACTIS; MEMBRANE PROTEINS; OPEN READING FRAMES; STREPTOCOCCUS AGALACTIAE;
EID: 84894286467     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.01014-13     Document Type: Article
Times cited : (32)
References (57)
  • 1
    • 0001240877 scopus 로고    scopus 로고
    • Group B streptococcal infections
    • Remington JS, Klein JO (ed), 5th ed. W. B. Saunders, Philadelphia, PA.
    • Edwards MS, Baker CJ. 2001. Group B streptococcal infections, p 1091-1156. In Remington JS, Klein JO (ed), Infectious diseases of the fetus and newborn, 5th ed. W. B. Saunders, Philadelphia, PA.
    • (2001) Infectious diseases of the fetus and newborn , pp. 1091-1156
    • Edwards, M.S.1    Baker, C.J.2
  • 2
    • 78649605964 scopus 로고    scopus 로고
    • Prevention of perinatal group B streptococcal disease-revised guidelines from CDC, 2010
    • Verani JR, McGee L, Schrag SJ. 2010. Prevention of perinatal group B streptococcal disease-revised guidelines from CDC, 2010. MMWR Recomm. Rep. 59:1-36.
    • (2010) MMWR Recomm. Rep. , vol.59 , pp. 1-36
    • Verani, J.R.1    McGee, L.2    Schrag, S.J.3
  • 3
    • 0034662445 scopus 로고    scopus 로고
    • The cyl genes of Streptococcus agalactiae are involved in the production of pigment
    • Spellerberg B, Martin S, Brandt C, Lutticken R. 2000. The cyl genes of Streptococcus agalactiae are involved in the production of pigment. FEMS Microbiol. Lett. 188:125-128. http://dx.doi.org/10.1111/j.1574-6968.2000.tb09182.x.
    • (2000) FEMS Microbiol. Lett. , vol.188 , pp. 125-128
    • Spellerberg, B.1    Martin, S.2    Brandt, C.3    Lutticken, R.4
  • 4
    • 0028235911 scopus 로고
    • Adherence of group B streptococci to cultured epithelial cells: roles of environmental factors and bacterial surface components
    • Tamura GS, Kuypers JM, Smith S, Raff H, Rubens CE. 1994. Adherence of group B streptococci to cultured epithelial cells: roles of environmental factors and bacterial surface components. Infect. Immun. 62:2450-2458.
    • (1994) Infect. Immun. , vol.62 , pp. 2450-2458
    • Tamura, G.S.1    Kuypers, J.M.2    Smith, S.3    Raff, H.4    Rubens, C.E.5
  • 5
    • 12844278673 scopus 로고    scopus 로고
    • Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens
    • Lindahl G, Stalhammar-Carlemalm M, Areschoug T. 2005. Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens. Clin. Microbiol. Rev. 18:102-127. http://dx.doi.org/10.1128 /CMR.18.1.102-127.2005.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 102-127
    • Lindahl, G.1    Stalhammar-Carlemalm, M.2    Areschoug, T.3
  • 6
    • 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. 2002. The group B streptococcal C5a peptidase is both a specific protease and an invasin. Infect. Immun. 70:2408-2413. http://dx.doi.org/10.1128/IAI.70.5.2408-2413.2002.
    • (2002) Infect. Immun. , vol.70 , pp. 2408-2413
    • Cheng, Q.1    Stafslien, D.2    Purushothaman, S.S.3    Cleary, P.4
  • 7
    • 2542558241 scopus 로고    scopus 로고
    • The novel fibrinogenbinding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells
    • Gutekunst H, Eikmanns BJ, Reinscheid DJ. 2004. The novel fibrinogenbinding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells. Infect. Immun. 72:3495-3504. http://dx.doi.org/10.1128 /IAI.72.6.3495-3504.2004.
    • (2004) Infect. Immun. , vol.72 , pp. 3495-3504
    • Gutekunst, H.1    Eikmanns, B.J.2    Reinscheid, D.J.3
  • 8
    • 84867589360 scopus 로고    scopus 로고
    • CsrRS and environmental pH regulate group B streptococcus adherence to human epithelial cells and extracellular matrix
    • Park SE, Jiang S, Wessels MR. 2012. CsrRS and environmental pH regulate group B streptococcus adherence to human epithelial cells and extracellular matrix. Infect. Immun. 80:3975-3984. http://dx.doi.org/10 .1128/IAI.00699-12.
    • (2012) Infect. Immun. , vol.80 , pp. 3975-3984
    • Park, S.E.1    Jiang, S.2    Wessels, M.R.3
  • 9
    • 33847719147 scopus 로고    scopus 로고
    • Evaluation of the ability of Streptococcus agalactiae strains isolated from genital and neonatal specimens to bind to human fibrinogen and correlation with characteristics of the fbsA and fbsB genes
    • Rosenau A, Martins K, Amor S, Gannier F, Lanotte P, van der Mee-Marquet N, Mereghetti L, Quentin R. 2007. Evaluation of the ability of Streptococcus agalactiae strains isolated from genital and neonatal specimens to bind to human fibrinogen and correlation with characteristics of the fbsA and fbsB genes. Infect. Immun. 75:1310-1317. http://dx.doi.org /10.1128/IAI.00996-06.
    • (2007) Infect. Immun. , vol.75 , pp. 1310-1317
    • Rosenau, A.1    Martins, K.2    Amor, S.3    Gannier, F.4    Lanotte, P.5    van der Mee-Marquet, N.6    Mereghetti, L.7    Quentin, R.8
  • 10
    • 35649005443 scopus 로고    scopus 로고
    • The surface protein Srr-1 of Streptococcus agalactiae binds human keratin 4 and promotes adherence to epithelial HEp-2 cells
    • Samen U, Eikmanns BJ, Reinscheid DJ, Borges F. 2007. The surface protein Srr-1 of Streptococcus agalactiae binds human keratin 4 and promotes adherence to epithelial HEp-2 cells. Infect. Immun. 75:5405-5414. http://dx.doi.org/10.1128/IAI.00717-07.
    • (2007) Infect. Immun. , vol.75 , pp. 5405-5414
    • Samen, U.1    Eikmanns, B.J.2    Reinscheid, D.J.3    Borges, F.4
  • 12
    • 7044247620 scopus 로고    scopus 로고
    • The fibrinogen receptor FbsA promotes adherence of Streptococcus agalactiae to human epithelial cells
    • Schubert A, Zakikhany K, Pietrocola G, Meinke A, Speziale P, Eikmanns BJ, Reinscheid DJ. 2004. The fibrinogen receptor FbsA promotes adherence of Streptococcus agalactiae to human epithelial cells. Infect. Immun. 72:6197-6205. http://dx.doi.org/10.1128/IAI.72.11.6197-6205 .2004.
    • (2004) Infect. Immun. , vol.72 , pp. 6197-6205
    • Schubert, A.1    Zakikhany, K.2    Pietrocola, G.3    Meinke, A.4    Speziale, P.5    Eikmanns, B.J.6    Reinscheid, D.J.7
  • 13
    • 0036428743 scopus 로고    scopus 로고
    • A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites
    • Schubert A, Zakikhany K, Schreiner M, Frank R, Spellerberg B, Eikmanns BJ, Reinscheid DJ. 2002. A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites. Mol. Microbiol. 46:557-569. http://dx.doi.org/10.1046 /j.1365-2958.2002.03177.x.
    • (2002) Mol. Microbiol. , vol.46 , pp. 557-569
    • Schubert, A.1    Zakikhany, K.2    Schreiner, M.3    Frank, R.4    Spellerberg, B.5    Eikmanns, B.J.6    Reinscheid, D.J.7
  • 15
    • 21544480286 scopus 로고    scopus 로고
    • Adherence to and invasion of human brain microvascular endothelial cells are promoted by fibrinogen-binding protein FbsA of Streptococcus agalactiae
    • Tenenbaum T, Bloier C, Adam R, Reinscheid DJ, Schroten H. 2005. Adherence to and invasion of human brain microvascular endothelial cells are promoted by fibrinogen-binding protein FbsA of Streptococcus agalactiae. Infect. Immun. 73:4404-4409. http://dx.doi.org/10.1128/IAI.73.7 .4404-4409.2005.
    • (2005) Infect. Immun. , vol.73 , pp. 4404-4409
    • Tenenbaum, T.1    Bloier, C.2    Adam, R.3    Reinscheid, D.J.4    Schroten, H.5
  • 16
    • 65549095152 scopus 로고    scopus 로고
    • The group B streptococcal serine-rich repeat 1 glycoprotein mediates penetration of the blood-brain barrier
    • van Sorge NM, Quach D, Gurney MA, Sullam PM, Nizet V, Doran KS.2009. The group B streptococcal serine-rich repeat 1 glycoprotein mediates penetration of the blood-brain barrier. J. Infect. Dis. 199:1479-1487. http://dx.doi.org/10.1086/598217.
    • (2009) J. Infect. Dis. , vol.199 , pp. 1479-1487
    • van Sorge, N.M.1    Quach, D.2    Gurney, M.A.3    Sullam, P.M.4    Nizet, V.5    Doran, K.S.6
  • 17
    • 0027992980 scopus 로고
    • Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria
    • Navarre WW, Schneewind O. 1994. Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol. Microbiol. 14:115-121. http://dx.doi.org/10.1111/j.1365-2958 .1994.tb01271.x.
    • (1994) Mol. Microbiol. , vol.14 , pp. 115-121
    • Navarre, W.W.1    Schneewind, O.2
  • 18
    • 0034973392 scopus 로고    scopus 로고
    • Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus
    • Mazmanian SK, Ton-That H, Schneewind O. 2001. Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus. Mol. Microbiol. 40:1049-1057. http://dx.doi.org/10.1046/j.1365-2958.2001.02 411.x.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1049-1057
    • Mazmanian, S.K.1    Ton-That, H.2    Schneewind, O.3
  • 21
    • 0027432395 scopus 로고
    • Stimulation of protective antibodies against type Ia and Ib group B streptococci by a type Ia polysaccharide-tetanus toxoid conjugate vaccine
    • Wessels MR, Paoletti LC, Rodewald AK, Michon F, DiFabio J, Jennings HJ, Kasper DL. 1993. Stimulation of protective antibodies against type Ia and Ib group B streptococci by a type Ia polysaccharide-tetanus toxoid conjugate vaccine. Infect. Immun. 61:4760-4766.
    • (1993) Infect. Immun. , vol.61 , pp. 4760-4766
    • Wessels, M.R.1    Paoletti, L.C.2    Rodewald, A.K.3    Michon, F.4    DiFabio, J.5    Jennings, H.J.6    Kasper, D.L.7
  • 24
    • 0016681271 scopus 로고
    • Multiple mouseprotective antibodies directed against group B streptococci. Special reference to antibodies effective against protein antigens
    • Lancefield RC, McCarty M, Everly WN. 1975. Multiple mouseprotective antibodies directed against group B streptococci. Special reference to antibodies effective against protein antigens. J. Exp. Med. 142:165-179.
    • (1975) J. Exp. Med. , vol.142 , pp. 165-179
    • Lancefield, R.C.1    McCarty, M.2    Everly, W.N.3
  • 25
    • 0023841503 scopus 로고
    • Lung antibacterial defense mechanisms in infant and adult rats: implications for the pathogenesis of group B streptococcal infections in neonatal lung
    • Martin TR, Rubens CE, Wilson CB. 1988. Lung antibacterial defense mechanisms in infant and adult rats: implications for the pathogenesis of group B streptococcal infections in neonatal lung. J. Infect. Dis. 157:91-100. http://dx.doi.org/10.1093/infdis/157.1.91.
    • (1988) J. Infect. Dis. , vol.157 , pp. 91-100
    • Martin, T.R.1    Rubens, C.E.2    Wilson, C.B.3
  • 26
    • 13244268247 scopus 로고    scopus 로고
    • Regulation of virulence by a two-component system in group B Streptococcus
    • Jiang SM, Cieslewicz MJ, Kasper DL, Wessels MR. 2005. Regulation of virulence by a two-component system in group B Streptococcus. J. Bacteriol. 187:1105-1113. http://dx.doi.org/10.1128/JB.187.3.1105-1113.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 1105-1113
    • Jiang, S.M.1    Cieslewicz, M.J.2    Kasper, D.L.3    Wessels, M.R.4
  • 27
    • 49749132761 scopus 로고    scopus 로고
    • Nisin inducible production of listeriolysin O in Lactococcus lactis NZ9000
    • Bahey-El-Din M, Griffin BT, Gahan CG. 2008. Nisin inducible production of listeriolysin O in Lactococcus lactis NZ9000. Microb. Cell Fact. 7:24. http://dx.doi.org/10.1186/1475-2859-7-24.
    • (2008) Microb. Cell Fact. , vol.7 , pp. 24
    • Bahey-El-Din, M.1    Griffin, B.T.2    Gahan, C.G.3
  • 28
    • 84861401525 scopus 로고    scopus 로고
    • Regulation and function of pilus island 1 in group B Streptococcus
    • Jiang S, Park SE, Yadav P, Paoletti LC, Wessels MR. 2012. Regulation and function of pilus island 1 in group B Streptococcus. J. Bacteriol. 194: 2479-2490. http://dx.doi.org/10.1128/JB.00202-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 2479-2490
    • Jiang, S.1    Park, S.E.2    Yadav, P.3    Paoletti, L.C.4    Wessels, M.R.5
  • 29
    • 67249101935 scopus 로고    scopus 로고
    • Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae
    • Konto-Ghiorghi Y, Mairey E, Mallet A, Dumenil G, Caliot E, Trieu-Cuot P, Dramsi S. 2009. Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae. PLoS Pathog. 5:e1000422. http://dx.doi.org/10.1371/journal.ppat.1000422.
    • (2009) PLoS Pathog. , vol.5
    • Konto-Ghiorghi, Y.1    Mairey, E.2    Mallet, A.3    Dumenil, G.4    Caliot, E.5    Trieu-Cuot, P.6    Dramsi, S.7
  • 31
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: recent updates to the protein domain annotation resource
    • Letunic I, Doerks T, Bork P. 2012. SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40:D302-305. http://dx.doi.org/10.1093/nar/gkr931.
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 33
    • 0028932607 scopus 로고
    • Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGAcontaining stop signals
    • Grentzmann G, Brechemier-Baey D, Heurgue-Hamard V, Buckingham RH. 1995. Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGAcontaining stop signals. J. Biol. Chem. 270:10595-10600.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10595-10600
    • Grentzmann, G.1    Brechemier-Baey, D.2    Heurgue-Hamard, V.3    Buckingham, R.H.4
  • 35
    • 84861162577 scopus 로고    scopus 로고
    • The CovS/CovR acid response regulator is required for intracellular survival of group B Streptococcus in macrophages
    • Cumley NJ, Smith LM, Anthony M, May RC. 2012. The CovS/CovR acid response regulator is required for intracellular survival of group B Streptococcus in macrophages. Infect. Immun. 80:1650-1661. http://dx.doi .org/10.1128/IAI.05443-11.
    • (2012) Infect. Immun. , vol.80 , pp. 1650-1661
    • Cumley, N.J.1    Smith, L.M.2    Anthony, M.3    May, R.C.4
  • 41
    • 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. http://dx.doi.org/10.1016/j .mib.2005.12.002.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 5-11
    • Hauck, C.R.1    Ohlsen, K.2
  • 42
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji ER, Slotboom DJ, Poolman B. 2003. Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim. Biophys. Acta 1610:97-108. http://dx.doi.org/10.1016/S0005-2736(02)00712-5.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 43
    • 27544451339 scopus 로고    scopus 로고
    • 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis
    • Mierau I, Kleerebezem M. 2005. 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis. Appl. Microbiol. Biotechnol. 68:705-717. http://dx.doi.org/10.1007/s00253-005-0107-6.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 705-717
    • Mierau, I.1    Kleerebezem, M.2
  • 44
    • 66049123975 scopus 로고    scopus 로고
    • Biofilm formation in clinical isolates of group B streptococci from north India
    • Kaur H, Kumar P, Ray P, Kaur J, Chakraborti A. 2009. Biofilm formation in clinical isolates of group B streptococci from north India. Microb. Pathog. 46:321-327. http://dx.doi.org/10.1016/j.micpath.2009.04.004.
    • (2009) Microb. Pathog. , vol.46 , pp. 321-327
    • Kaur, H.1    Kumar, P.2    Ray, P.3    Kaur, J.4    Chakraborti, A.5
  • 45
    • 79960404091 scopus 로고    scopus 로고
    • The FbaB-type fibronectin-binding protein of Streptococcus pyogenes promotes specific invasion into endothelial cells
    • Amelung S, Nerlich A, Rohde M, Spellerberg B, Cole JN, Nizet V, Chhatwal GS, Talay SR. 2011. The FbaB-type fibronectin-binding protein of Streptococcus pyogenes promotes specific invasion into endothelial cells. Cell. Microbiol. 13:1200-1211. http://dx.doi.org/10.1111/j.1462-5822.2011.01610.x.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1200-1211
    • Amelung, S.1    Nerlich, A.2    Rohde, M.3    Spellerberg, B.4    Cole, J.N.5    Nizet, V.6    Chhatwal, G.S.7    Talay, S.R.8
  • 46
    • 34247272544 scopus 로고    scopus 로고
    • Detection of genes encoding internalization-associated proteins in Streptococcus pyogenes isolates from patients with invasive diseases and asymptomatic carriers
    • Baldassarri L, Creti R, Imperi M, Recchia S, Pataracchia M, Orefici G.2007. Detection of genes encoding internalization-associated proteins in Streptococcus pyogenes isolates from patients with invasive diseases and asymptomatic carriers. J. Clin. Microbiol. 45:1284-1287. http://dx.doi .org/10.1128/JCM.02119-06.
    • (2007) J. Clin. Microbiol. , vol.45 , pp. 1284-1287
    • Baldassarri, L.1    Creti, R.2    Imperi, M.3    Recchia, S.4    Pataracchia, M.5    Orefici, G.6
  • 47
    • 0033791977 scopus 로고    scopus 로고
    • Staphylococcal fibronectin binding protein interacts with heat shock protein 60 and integrins: role in internalization by epithelial cells
    • Dziewanowska K, Carson AR, Patti JM, Deobald CF, Bayles KW, Bohach GA. 2000. Staphylococcal fibronectin binding protein interacts with heat shock protein 60 and integrins: role in internalization by epithelial cells. Infect. Immun. 68:6321-6328. http://dx.doi.org/10.1128/IAI.68 .11.6321-6328.2000.
    • (2000) Infect. Immun. , vol.68 , pp. 6321-6328
    • Dziewanowska, K.1    Carson, A.R.2    Patti, J.M.3    Deobald, C.F.4    Bayles, K.W.5    Bohach, G.A.6
  • 48
    • 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. http://dx.doi.org/10.1128/IAI.00300-08.
    • (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
  • 49
    • 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. http://dx.doi.org/10.1078 /0171-9335-00104.
    • (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
  • 50
    • 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. http: //dx.doi.org/10.1111/j.1574-6968.1999.tb08783.x.
    • (1999) FEMS Microbiol. Lett , vol.180 , pp. 103-109
    • Lammers, A.1    Nuijten, P.J.2    Smith, H.E.3
  • 52
    • 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. http://dx.doi.org /10.1016/j.micinf.2006.03.011.
    • (2006) Microbes Infect. , vol.8 , pp. 2291-2298
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 54
    • 84874986448 scopus 로고    scopus 로고
    • Pleiotropic virulence factor-Streptococcus pyogenes fibronectin-binding proteins
    • 29 November
    • Yamaguchi M, Terao Y, Kawabata S. 29 November 2012. Pleiotropic virulence factor-Streptococcus pyogenes fibronectin-binding proteins. Cell. Microbiol. http://dx.doi.org/10.1111/cmi.12083.
    • (2012) Cell. Microbiol
    • Yamaguchi, M.1    Terao, Y.2    Kawabata, S.3
  • 55
    • 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. http://dx.doi.org/10.1053 /jinf.2000.0657.
    • (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
  • 56
    • 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. http://dx.doi.org/10.1128/IAI.70.6.2869-2876 .2002.
    • (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
  • 57
    • 0027208133 scopus 로고
    • An M protein with a single C repeat prevents phagocytosis of Streptococcus pyogenes: use of a temperature-sensitive shuttle vector to deliver homologous sequences to the chromosome of S. pyogenes
    • Perez-Casal J, Price JA, Maguin E, Scott JR. 1993. An M protein with a single C repeat prevents phagocytosis of Streptococcus pyogenes: use of a temperature-sensitive shuttle vector to deliver homologous sequences to the chromosome of S. pyogenes. Mol. Microbiol. 8:809-819. http://dx.doi .org/10.1111/j.1365-2958.1993.tb01628.x.
    • (1993) Mol. Microbiol. , vol.8 , pp. 809-819
    • Perez-Casal, J.1    Price, J.A.2    Maguin, E.3    Scott, J.R.4

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.