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Volumn 60, Issue 6, 2006, Pages 1401-1413

Assembly and role of pili in group B streptococci

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; MEMBRANE PROTEIN; PILIN; SORTASE;

EID: 33744485570     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05190.x     Document Type: Article
Times cited : (203)

References (53)
  • 1
    • 0036207211 scopus 로고    scopus 로고
    • Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs
    • Barnett, T.C. Scott, J.R. 2002 Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs. J Bacteriol 184: 2181 2191.
    • (2002) J Bacteriol , vol.184 , pp. 2181-2191
    • Barnett, T.C.1    Scott, J.R.2
  • 3
    • 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, J.D., Harris, T.O., Tamura, G.S. Rubens, C.E. 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
  • 4
    • 0027151798 scopus 로고
    • High-efficiency gene inactivation and replacement system for gram-positive bacteria
    • Biswas, I., Gruss, A., Ehrlich, S.D. Maguin, E. 1993 High-efficiency gene inactivation and replacement system for gram-positive bacteria. J Bacteriol 175: 3628 3635.
    • (1993) J Bacteriol , vol.175 , pp. 3628-3635
    • Biswas, I.1    Gruss, A.2    Ehrlich, S.D.3    Maguin, E.4
  • 5
    • 0022586474 scopus 로고
    • A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii
    • Brennan, M.J., Cisar, J.O. Sandberg, A.L. 1986 A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii. Infect Immun 52: 840 845.
    • (1986) Infect Immun , vol.52 , pp. 840-845
    • Brennan, M.J.1    Cisar, J.O.2    Sandberg, A.L.3
  • 7
    • 0036117970 scopus 로고    scopus 로고
    • The group B streptococcal C5a peptidase is both a specific protease and an invasin
    • Cheng, O., Stafslien, D., Purushothaman, S.S. Cleary, P. 2002 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, O.1    Stafslien, D.2    Purushothaman, S.S.3    Cleary, P.4
  • 8
    • 0035403501 scopus 로고    scopus 로고
    • The mannose-sensitive hemagluttinin of Vibrio cholerae promotes adherence to zooplancton
    • Chiavelli, D.A., Marsh, J.W. Taylor, R.K. 2001 The mannose-sensitive hemagluttinin of Vibrio cholerae promotes adherence to zooplancton. Appl Environ Microbiol 67: 3220 3225.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3220-3225
    • Chiavelli, D.A.1    Marsh, J.W.2    Taylor, R.K.3
  • 9
    • 2142808787 scopus 로고    scopus 로고
    • A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria
    • Comfort, D. Clubb, R.T. 2004 A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria. Infect Immun 72: 2710 2722.
    • (2004) Infect Immun , vol.72 , pp. 2710-2722
    • Comfort, D.1    Clubb, R.T.2
  • 10
    • 0034625048 scopus 로고    scopus 로고
    • Sortase, a universal target for therapeutic agents against gram-positive bacteria?
    • Cossart, P. Jonquieres, R. 2000 Sortase, a universal target for therapeutic agents against gram-positive bacteria? Proc Natl Acad Sci USA 97: 5013 5015.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5013-5015
    • Cossart, P.1    Jonquieres, R.2
  • 11
    • 16844372650 scopus 로고    scopus 로고
    • Sorting sortases: A nomenclature proposal for the various sortases of Gram-positive bacteria
    • Dramsi, S., Trieu-Cuot, P. Bierne, H. 2005 Sorting sortases: a nomenclature proposal for the various sortases of Gram-positive bacteria. Res Microbiol 156: 289 297.
    • (2005) Res Microbiol , vol.156 , pp. 289-297
    • Dramsi, S.1    Trieu-Cuot, P.2    Bierne, H.3
  • 12
    • 0025077034 scopus 로고
    • Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci
    • Fischetti, V.A., Pancholi, V. Schneewind, O. 1990 Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol Microbiol 4: 1603 1605.
    • (1990) Mol Microbiol , vol.4 , pp. 1603-1605
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 13
    • 0031578913 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of the superoxide dismutase gene from Streptococcus agalactiae
    • Gaillot, O., Poyart, C., Berche, P. Trieu-Cuot, P. 1997 Molecular characterization and expression analysis of the superoxide dismutase gene from Streptococcus agalactiae. Gene 204: 213 218.
    • (1997) Gene , vol.204 , pp. 213-218
    • Gaillot, O.1    Poyart, C.2    Berche, P.3    Trieu-Cuot, P.4
  • 14
    • 0023757544 scopus 로고    scopus 로고
    • Adsorbed salivary proline-rich protein 1 and statherin: Receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces
    • Gibbons, R.J., Hay, D.I., Cisar, J.O. Clark, W.B. 1998 Adsorbed salivary proline-rich protein 1 and statherin: receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces. Infect Immun 56: 2990 2993.
    • (1998) Infect Immun , vol.56 , pp. 2990-2993
    • Gibbons, R.J.1    Hay, D.I.2    Cisar, J.O.3    Clark, W.B.4
  • 15
    • 0030814152 scopus 로고    scopus 로고
    • Role of pili in Haemophilus influenzae adherence and colonization
    • Gilsdorf, J.R., McCrea, K.W. Marrs, C.F. 1997 Role of pili in Haemophilus influenzae adherence and colonization. Infect Immun 65: 2997 3002.
    • (1997) Infect Immun , vol.65 , pp. 2997-3002
    • Gilsdorf, J.R.1    McCrea, K.W.2    Marrs, C.F.3
  • 16
    • 18644378733 scopus 로고    scopus 로고
    • Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease
    • Glaser, P., Rusniok, C., Buchrieser, C., Chevalier, F., Frangeul, L., Msadek, T., et al. 2002 Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease. Mol Microbiol 45: 1499 1513.
    • (2002) Mol Microbiol , vol.45 , pp. 1499-1513
    • Glaser, P.1    Rusniok, C.2    Buchrieser, C.3    Chevalier, F.4    Frangeul, L.5    Msadek, T.6
  • 17
    • 0042324298 scopus 로고    scopus 로고
    • Analysis of RogB-controlled virulence mechanisms and gene repression in Streptococcus agalactiae
    • Gutekunst, H., Eikmanns, B.J. Reinscheid, D.J. 2003 Analysis of RogB-controlled virulence mechanisms and gene repression in Streptococcus agalactiae. Infect Immun 71: 5056 5064.
    • (2003) Infect Immun , vol.71 , pp. 5056-5064
    • Gutekunst, H.1    Eikmanns, B.J.2    Reinscheid, D.J.3
  • 18
    • 2542558241 scopus 로고    scopus 로고
    • The novel fibrinogen-binding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells
    • Gutekunst, H., Eikmanns, B.J. Reinscheid, D.J. 2004 The novel fibrinogen-binding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells. Infect Immun 72: 3495 3504.
    • (2004) Infect Immun , vol.72 , pp. 3495-3504
    • Gutekunst, H.1    Eikmanns, B.J.2    Reinscheid, D.J.3
  • 19
    • 0037224589 scopus 로고    scopus 로고
    • Transcriptional regulation in the Streptococcus pneumoniae rlrA pathogenicity islet by RlrA
    • Hava, D.L., Hemsley, C.J. Camilli, A. 2003 Transcriptional regulation in the Streptococcus pneumoniae rlrA pathogenicity islet by RlrA. J Bacteriol 185: 413 421.
    • (2003) J Bacteriol , vol.185 , pp. 413-421
    • Hava, D.L.1    Hemsley, C.J.2    Camilli, A.3
  • 20
    • 0035932982 scopus 로고    scopus 로고
    • Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus
    • Ilangovan, U., Ton-That, H., Iwahara, J., Schneewind, O. Clubb, R.T. 2001 Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proc Natl Acad Sci USA 98: 6056 6061.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6056-6061
    • Ilangovan, U.1    Ton-That, H.2    Iwahara, J.3    Schneewind, O.4    Clubb, R.T.5
  • 21
    • 0037674820 scopus 로고    scopus 로고
    • Virulence factor regulation and regulatory networks in Streptococcus pyogenes and their impact on pathogen-host interactions
    • Kreikemeyer, B., McIver, K.S. Podbielski, A. 2003 Virulence factor regulation and regulatory networks in Streptococcus pyogenes and their impact on pathogen-host interactions. Trends Microbiol 11: 224 232.
    • (2003) Trends Microbiol , vol.11 , pp. 224-232
    • Kreikemeyer, B.1    McIver, K.S.2    Podbielski, A.3
  • 22
    • 21144462780 scopus 로고    scopus 로고
    • The SrtA of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine
    • Lalioui, L., Pellegrini, E., Dramsi, S., Baptista, M., Bourgeois, N., Doucet-Populaire, F., et al. 2005 The SrtA of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine. Infect Immun 73: 3342 3350.
    • (2005) Infect Immun , vol.73 , pp. 3342-3350
    • Lalioui, L.1    Pellegrini, E.2    Dramsi, S.3    Baptista, M.4    Bourgeois, N.5    Doucet-Populaire, F.6
  • 24
    • 33645512064 scopus 로고    scopus 로고
    • RrgA and RrgB are components of a multisubunit pilus encoded by the Streptococcus pneumoniae rlrA pathogenicity islet
    • Lemieux, J., Hava, D.L., Basset, A. Camilli, A. 2006 RrgA and RrgB are components of a multisubunit pilus encoded by the Streptococcus pneumoniae rlrA pathogenicity islet. Infect Immun 74: 2453 2456.
    • (2006) Infect Immun , vol.74 , pp. 2453-2456
    • Lemieux, J.1    Hava, D.L.2    Basset, A.3    Camilli, A.4
  • 25
    • 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.
    • (2005) Clin Microbiol Rev , vol.18 , pp. 102-127
    • Lindahl, G.1    Stalhammar-Carlemalm, M.2    Areschoug, T.3
  • 26
    • 0011291359 scopus 로고
    • Gene products specifying adhesion of uropathogenic Escherichia coli are minor components of pili
    • Lindberg, F., Lund, B. Normark, S. 1986 Gene products specifying adhesion of uropathogenic Escherichia coli are minor components of pili. Proc Natl Acad Sci USA 83: 1891 1895.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1891-1895
    • Lindberg, F.1    Lund, B.2    Normark, S.3
  • 27
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak, K.J. Schmittgen, T.D. 2001 Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402 408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 28
    • 0023929025 scopus 로고
    • A polysaccharide from Streptococcus sanguis 34 that inhibits coaggregation of S. sanguis 34 with Actinomyces viscosus T14V
    • McIntire, F.C., Crosby, L.K., Vatter, A.E., Cisar, J.O., McNeil, M.R., Bush, C.A., et al. 1988 A polysaccharide from Streptococcus sanguis 34 that inhibits coaggregation of S. sanguis 34 with Actinomyces viscosus T14V. J Bacteriol 170: 2229 2235.
    • (1988) J Bacteriol , vol.170 , pp. 2229-2235
    • McIntire, F.C.1    Crosby, L.K.2    Vatter, A.E.3    Cisar, J.O.4    McNeil, M.R.5    Bush, C.A.6
  • 29
    • 21644481459 scopus 로고    scopus 로고
    • Identification of a universal Group B streptococcus vaccine by multiple genome screen
    • Maione, D., Margarit, I., Rinaudo, C.D., Masignani, V., Mora, M., Scarselli, M., et al. 2005 Identification of a universal Group B streptococcus vaccine by multiple genome screen. Science 309: 148 150.
    • (2005) Science , vol.309 , pp. 148-150
    • Maione, D.1    Margarit, I.2    Rinaudo, C.D.3    Masignani, V.4    Mora, M.5    Scarselli, M.6
  • 30
    • 0035067086 scopus 로고    scopus 로고
    • The AraC transcriptional activators
    • Martin, R.G. Rosner, J.L. 2001 The AraC transcriptional activators. Curr Opin Microbiol 4: 132 137.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 132-137
    • Martin, R.G.1    Rosner, J.L.2
  • 31
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S.K., Liu, G., Ton-That, H. Schneewind, O. 1999 Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285: 760 763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 32
    • 0037133213 scopus 로고    scopus 로고
    • An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis
    • Mazmanian, S.K., Ton-That, H., Su, K. Schneewind, O. 2002 An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc Natl Acad Sci USA 99: 2293 2298.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2293-2298
    • Mazmanian, S.K.1    Ton-That, H.2    Su, K.3    Schneewind, O.4
  • 33
    • 27344448129 scopus 로고    scopus 로고
    • Group a Streptococcus produce pili-like structures containing protective antigens and Lancefield T antigens
    • Mora, M., Bensi, G., Capo, S., Falugi, F., Zingaretti, C., Manetti, A.G., et al. 2005 Group A Streptococcus produce pili-like structures containing protective antigens and Lancefield T antigens. Proc Natl Acad Sci USA 102: 15641 15646.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15641-15646
    • Mora, M.1    Bensi, G.2    Capo, S.3    Falugi, F.4    Zingaretti, C.5    Manetti, A.G.6
  • 34
    • 0026027810 scopus 로고
    • Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase
    • Munier, H., Gilles, A.M., Glaser, P., Krin, E., Danchin, A., Sarfati, R. Barzu, O. 1991 Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase. Eur J Biochem 196: 469 474.
    • (1991) Eur J Biochem , vol.196 , pp. 469-474
    • Munier, H.1    Gilles, A.M.2    Glaser, P.3    Krin, E.4    Danchin, A.5    Sarfati, R.6    Barzu, O.7
  • 36
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre, W.W. Schneewind, O. 1999 Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev 63: 174 229.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 37
    • 6344275007 scopus 로고    scopus 로고
    • Modulation of AraC family member activity by protein ligands
    • Plano, G.V. 2004 Modulation of AraC family member activity by protein ligands. Mol Microbiol 54: 287 290.
    • (2004) Mol Microbiol , vol.54 , pp. 287-290
    • Plano, G.V.1
  • 38
    • 0031568919 scopus 로고    scopus 로고
    • Product differentiation by analysis of DNA melting curves during the polymerase chain reaction
    • Ririe, K.M., Rasmussen, R.P. Wittwer, C.T. 1997 Product differentiation by analysis of DNA melting curves during the polymerase chain reaction. Anal Biochem 245: 154 160.
    • (1997) Anal Biochem , vol.245 , pp. 154-160
    • Ririe, K.M.1    Rasmussen, R.P.2    Wittwer, C.T.3
  • 41
    • 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, B.J. Reinscheid, D.J. 2002 A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites. Mol Microbiol 46: 557 569.
    • (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
  • 42
    • 0032935929 scopus 로고    scopus 로고
    • Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition
    • Spellerberg, B., Pohl, B., Haase, G., Martin, S., Weber-Heynemann, J. Lutticken, R. 1999 Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition. J Bacteriol 181: 3212 3219.
    • (1999) J Bacteriol , vol.181 , pp. 3212-3219
    • Spellerberg, B.1    Pohl, B.2    Haase, G.3    Martin, S.4    Weber-Heynemann, J.5    Lutticken, R.6
  • 43
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W. Moffatt, B.A. 1986 Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189: 113 130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 44
    • 0037125989 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae
    • Tettelin, H., Masignani, V., Cieslewicz, M.J., Eisen, J.A., Peterson, S., Wessels, M.R., et al. 2002 Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae. Proc Natl Acad Sci USA 99: 12391 12396.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12391-12396
    • Tettelin, H.1    Masignani, V.2    Cieslewicz, M.J.3    Eisen, J.A.4    Peterson, S.5    Wessels, M.R.6
  • 45
    • 25444524604 scopus 로고    scopus 로고
    • Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: Implications for the microbial 'pan-genome'
    • Tettelin, H., Masignani, V., Cieslewicz, M.J., Donati, C., Medini, D., Ward, N.L., et al. 2005 Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: implications for the microbial 'pan-genome'. Proc Natl Acad Sci USA 102: 13950 13955.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13950-13955
    • Tettelin, H.1    Masignani, V.2    Cieslewicz, M.J.3    Donati, C.4    Medini, D.5    Ward, N.L.6
  • 46
    • 0345689425 scopus 로고    scopus 로고
    • Assembly of pili on the surface of Corynebacterium diphtheriae
    • Ton-That, H. Schneewind, O. 2003 Assembly of pili on the surface of Corynebacterium diphtheriae. Mol Microbiol 50: 1429 1438.
    • (2003) Mol Microbiol , vol.50 , pp. 1429-1438
    • Ton-That, H.1    Schneewind, O.2
  • 47
    • 2042470134 scopus 로고    scopus 로고
    • Assembly of pili in Gram-positive bacteria
    • Ton-That, H. Schneewind, O. 2004 Assembly of pili in Gram-positive bacteria. Trends Microbiol 12: 228 234.
    • (2004) Trends Microbiol , vol.12 , pp. 228-234
    • Ton-That, H.1    Schneewind, O.2
  • 48
    • 0034737451 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates
    • Ton-That, H., Mazmanian, S.K., Faull, K.F. Schneewind, O. 2000 Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates. J Biol Chem 275: 9876 9881.
    • (2000) J Biol Chem , vol.275 , pp. 9876-9881
    • Ton-That, H.1    Mazmanian, S.K.2    Faull, K.F.3    Schneewind, O.4
  • 49
    • 0036510385 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis
    • Ton-That, H., Mazmanian, S.K., Alksne, L. Schneewind, O. 2002 Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis. J Biol Chem 277: 7447 7452.
    • (2002) J Biol Chem , vol.277 , pp. 7447-7452
    • Ton-That, H.1    Mazmanian, S.K.2    Alksne, L.3    Schneewind, O.4
  • 50
    • 3142559796 scopus 로고    scopus 로고
    • Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae
    • Ton-That, H., Marraffini, L.A. Schneewind, O. 2004 Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae. Mol Microbiol 53: 251 261.
    • (2004) Mol Microbiol , vol.53 , pp. 251-261
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 51
    • 0035022986 scopus 로고    scopus 로고
    • Molecular strategies for fimbrial expression and assembly
    • Wu, H. Fives-Taylor, P.M. 2001 Molecular strategies for fimbrial expression and assembly. Crit Rev Oral Biol Medical 12: 101 115.
    • (2001) Crit Rev Oral Biol Medical , vol.12 , pp. 101-115
    • Wu, H.1    Fives-Taylor, P.M.2
  • 52
    • 0025272711 scopus 로고
    • Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp
    • Yeung, M.K. Cisar, J.O. 1990 Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp. J Bacteriol 172: 2462 2468.
    • (1990) J Bacteriol , vol.172 , pp. 2462-2468
    • Yeung, M.K.1    Cisar, J.O.2
  • 53
    • 0030954094 scopus 로고    scopus 로고
    • Synthesis and function of Actinomyces naeslundii T14V type 1 fimbriae require the expression of additional fimbria-associated genes
    • Yeung, M.K. Ragsdale, P.A. 1997 Synthesis and function of Actinomyces naeslundii T14V type 1 fimbriae require the expression of additional fimbria-associated genes. Infect Immun 65: 2629 2639.
    • (1997) Infect Immun , vol.65 , pp. 2629-2639
    • Yeung, M.K.1    Ragsdale, P.A.2


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