메뉴 건너뛰기




Volumn 3, Issue 4, 2003, Pages 191-200

Molecular basis of group A streptococcal virulence

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; BINDING PROTEIN; CYTOKINE; FIBRONECTIN; HYALURONIC ACID; M PROTEIN; STREPTOCOCCUS VACCINE; VIRULENCE FACTOR;

EID: 0037381631     PISSN: 14733099     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1473-3099(03)00576-0     Document Type: Review
Times cited : (413)

References (149)
  • 1
    • 0036680109 scopus 로고    scopus 로고
    • Epidemiology of invasive group A streptococcus disease in the United States, 1995-1999
    • O'Brien KL, Beall B, Barrett NL, et al. Epidemiology of invasive group A streptococcus disease in the United States, 1995-1999. Clin Infect Dis 2002; 35: 268-76.
    • (2002) Clin Infect Dis , vol.35 , pp. 268-276
    • O'Brien, K.L.1    Beall, B.2    Barrett, N.L.3
  • 2
    • 0017647716 scopus 로고
    • Purification and properties of M protein extracted from group A streptococci with pepsin: Covalent structure of the amino terminal region of type 24 M antigen
    • Beachey EH, Stollerman GH, Chiang EY, Chiang TM, Seyer JM, Kang AH. Purification and properties of M protein extracted from group A streptococci with pepsin: covalent structure of the amino terminal region of type 24 M antigen. J Exp Med 1977; 145: 1469-83.
    • (1977) J Exp Med , vol.145 , pp. 1469-1483
    • Beachey, E.H.1    Stollerman, G.H.2    Chiang, E.Y.3    Chiang, T.M.4    Seyer, J.M.5    Kang, A.H.6
  • 3
    • 0025761098 scopus 로고
    • Streptococcal M protein
    • Fischetti VA. Streptococcal M protein. Sci Am 1991; 264: 58-65.
    • (1991) Sci Am , vol.264 , pp. 58-65
    • Fischetti, V.A.1
  • 5
    • 0036133503 scopus 로고    scopus 로고
    • Extension of the Lancefield classification for group A streptococci by addition of 22 new M protein gene sequence types from clinical isolates: emm103 to emm124
    • Facklam RF, Martin DR, Lovgren M, et al. Extension of the Lancefield classification for group A streptococci by addition of 22 new M protein gene sequence types from clinical isolates: emm103 to emm124. Clin Infect Dis 2002; 34: 28-38.
    • (2002) Clin Infect Dis , vol.34 , pp. 28-38
    • Facklam, R.F.1    Martin, D.R.2    Lovgren, M.3
  • 6
    • 0028951369 scopus 로고
    • Genetic diversity and relationships among Streptococcus pyogenes strains expressing serotype M1 protein: Recent intercontinental spread of a subclone causing episodes of invasive disease
    • Musser JM, Kapur V, Szeto J, Pan X, Swanson DS, Martin DR. Genetic diversity and relationships among Streptococcus pyogenes strains expressing serotype M1 protein: recent intercontinental spread of a subclone causing episodes of invasive disease. Infect Immun 1995; 63: 994-1003.
    • (1995) Infect Immun , vol.63 , pp. 994-1003
    • Musser, J.M.1    Kapur, V.2    Szeto, J.3    Pan, X.4    Swanson, D.S.5    Martin, D.R.6
  • 7
    • 0018728788 scopus 로고
    • Alternate complement pathway activation by group A streptococci: Role of M-protein
    • Bisno AL. Alternate complement pathway activation by group A streptococci: role of M-protein. Infect Immun 1979; 26: 1172-76.
    • (1979) Infect Immun , vol.26 , pp. 1172-1176
    • Bisno, A.L.1
  • 8
    • 0343017792 scopus 로고
    • Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H
    • Horstmann RD, Sievertsen HJ, Knobloch J, Fischetti VA. Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc Natl Acad Sci USA 1988; 85: 1657-61.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1657-1661
    • Horstmann, R.D.1    Sievertsen, H.J.2    Knobloch, J.3    Fischetti, V.A.4
  • 9
    • 0032211139 scopus 로고    scopus 로고
    • Role of the hypervariable region in streptococcal M proteins: Binding of a human complement inhibitor
    • Johnsson E, Berggard K, Kotarsky H, et al. Role of the hypervariable region in streptococcal M proteins: binding of a human complement inhibitor. J Immunol 1998; 161: 4894-901.
    • (1998) J Immunol , vol.161 , pp. 4894-4901
    • Johnsson, E.1    Berggard, K.2    Kotarsky, H.3
  • 10
    • 0035723519 scopus 로고    scopus 로고
    • Group A streptococcal phagocytosis resistance is independent of complement factor H and factor H-like protein 1 binding
    • Kotarsky H, Gustafsson M, Svensson HG, Zipfel PF, Truedsson L, Sjobring U. Group A streptococcal phagocytosis resistance is independent of complement factor H and factor H-like protein 1 binding. Mol Microbiol 2001; 41: 817-26.
    • (2001) Mol Microbiol , vol.41 , pp. 817-826
    • Kotarsky, H.1    Gustafsson, M.2    Svensson, H.G.3    Zipfel, P.F.4    Truedsson, L.5    Sjobring, U.6
  • 11
    • 0034768706 scopus 로고    scopus 로고
    • Binding of human C4BP to the hypervariable region of M protein: A molecular mechanism of phagocytosis resistance in Streptococcus pyogenes
    • Berggard K, Johnsson E, Morfeldt E, Persson J, Stalhammar-Carlemalm M, Lindahl G. Binding of human C4BP to the hypervariable region of M protein: a molecular mechanism of phagocytosis resistance in Streptococcus pyogenes. Mol Microbiol 2001; 42: 539-51.
    • (2001) Mol Microbiol , vol.42 , pp. 539-551
    • Berggard, K.1    Johnsson, E.2    Morfeldt, E.3    Persson, J.4    Stalhammar-Carlemalm, M.5    Lindahl, G.6
  • 12
    • 0342265104 scopus 로고    scopus 로고
    • Assessment of the interaction of human complement regulatory proteins with group A streptococcus. Identification of a high-affinity group A streptococcus binding site in FHL-1
    • Perez-Caballero D, Alberti S, Vivanco F, Sanchez-Corral P, Rodriguez dC. Assessment of the interaction of human complement regulatory proteins with group A streptococcus. Identification of a high-affinity group A streptococcus binding site in FHL-1. Eur J Immunol 2000; 30: 1243-53.
    • (2000) Eur J Immunol , vol.30 , pp. 1243-1253
    • Perez-Caballero, D.1    Alberti, S.2    Vivanco, F.3    Sanchez-Corral, P.4    Rodriguez, D.C.5
  • 13
    • 0022295839 scopus 로고
    • Inhibition of complement-mediated opsonization and phagocytosis of Streptococcus pyogenes by D fragments of fibrinogen and fibrin bound to cell surface M protein
    • Whitnack E, Beachey EH. Inhibition of complement-mediated opsonization and phagocytosis of Streptococcus pyogenes by D fragments of fibrinogen and fibrin bound to cell surface M protein. J Exp Med 1985; 162: 1983-97.
    • (1985) J Exp Med , vol.162 , pp. 1983-1997
    • Whitnack, E.1    Beachey, E.H.2
  • 14
    • 0029922220 scopus 로고    scopus 로고
    • Hyaluronate capsule and surface M protein in resistance to opsonization of group A streptococci
    • Dale JB, Washburn RG, Marques MB, Wessels MR. Hyaluronate capsule and surface M protein in resistance to opsonization of group A streptococci. Infect Immun 1996; 64:1495-501.
    • (1996) Infect Immun , vol.64 , pp. 1495-1501
    • Dale, J.B.1    Washburn, R.G.2    Marques, M.B.3    Wessels, M.R.4
  • 15
    • 0344559091 scopus 로고
    • Management of streptococcal infections and prevention of rheumatic fever: The changing scene
    • Sande MA, Hudson LD, Root RK, eds. New York: Churchill Livingston
    • Bisno AL. Management of streptococcal infections and prevention of rheumatic fever: the changing scene. In: Sande MA, Hudson LD, Root RK, eds. Contemporary issues in infectious diseases, vol 5. Respiratory infections. New York: Churchill Livingston; 1986: 217-34.
    • (1986) Contemporary Issues in Infectious Diseases, Vol 5. Respiratory Infections , vol.5 , pp. 217-234
    • Bisno, A.L.1
  • 16
    • 0029150445 scopus 로고
    • A single emm gene-specific oligonucleotide probe does not recognise all members of the Streptococcus pyogenes M type 1
    • Penney TJ, Martin DR, Williams LC, de Malmanche SA, Bergquist PL. A single emm gene-specific oligonucleotide probe does not recognise all members of the Streptococcus pyogenes M type 1. FEMS Microbiol Lett 1995; 130: 145-50.
    • (1995) FEMS Microbiol Lett , vol.130 , pp. 145-150
    • Penney, T.J.1    Martin, D.R.2    Williams, L.C.3    De Malmanche, S.A.4    Bergquist, P.L.5
  • 17
    • 0029442715 scopus 로고
    • Genetic diversity and relationships among serotype M1 strains of Streptococcus pyogenes
    • Musser JM, Kapur V, Szeto J, Pan X, Swanson DS, Martin DR. Genetic diversity and relationships among serotype M1 strains of Streptococcus pyogenes. Dev Biol Stand 1995; 85: 209-13.
    • (1995) Dev Biol Stand , vol.85 , pp. 209-213
    • Musser, J.M.1    Kapur, V.2    Szeto, J.3    Pan, X.4    Swanson, D.S.5    Martin, D.R.6
  • 18
    • 0028648266 scopus 로고
    • Protective immunity to the group A streptococcus may be only strain specific
    • de Malmanche SA, Martin DR. Protective immunity to the group A streptococcus may be only strain specific. Med Microbiol Immunol 1994; 183: 299-306.
    • (1994) Med Microbiol Immunol , vol.183 , pp. 299-306
    • De Malmanche, S.A.1    Martin, D.R.2
  • 19
    • 0030055805 scopus 로고    scopus 로고
    • M-related protein (Mrp) contributes to group A streptococcal resistance to phagocytosis by human granulocytes
    • Podbielski A, Schnitzler N, Beyhs P, Boyle MDP. M-related protein (Mrp) contributes to group A streptococcal resistance to phagocytosis by human granulocytes. Mol Microbiol 1996; 19: 429-41.
    • (1996) Mol Microbiol , vol.19 , pp. 429-441
    • Podbielski, A.1    Schnitzler, N.2    Beyhs, P.3    Boyle, M.D.P.4
  • 20
    • 0032412103 scopus 로고    scopus 로고
    • Impact of M49, Mrp, Enn, and C5a peptidase proteins on colonization of the mouse oral mucosa by Streptococcus pyogenes
    • Ji Y, Schnitzler N, DeMaster E, Cleary P. Impact of M49, Mrp, Enn, and C5a peptidase proteins on colonization of the mouse oral mucosa by Streptococcus pyogenes. Infect Immun 1998; 66: 5399-405.
    • (1998) Infect Immun , vol.66 , pp. 5399-5405
    • Ji, Y.1    Schnitzler, N.2    DeMaster, E.3    Cleary, P.4
  • 22
    • 0035657925 scopus 로고    scopus 로고
    • Evasion of human innate and acquired immunity by a bacterial homolog of CD 11 b that inhibits opsonophagocytosis
    • Lei B, DeLeo FR, Hoe NP, et al. Evasion of human innate and acquired immunity by a bacterial homolog of CD 11 b that inhibits opsonophagocytosis. Nat Med 2001; 7: 1298-305.
    • (2001) Nat Med , vol.7 , pp. 1298-1305
    • Lei, B.1    DeLeo, F.R.2    Hoe, N.P.3
  • 23
    • 0029099312 scopus 로고
    • Hyaluronic acid synthesis operon (has) expression in group A streptococci
    • Crater DL, van de Rijn I. Hyaluronic acid synthesis operon (has) expression in group A streptococci. J Biol Chem 1995; 270: 18452-58.
    • (1995) J Biol Chem , vol.270 , pp. 18452-18458
    • Crater, D.L.1    Van de Rijn, I.2
  • 24
    • 0031892902 scopus 로고    scopus 로고
    • Structure of the has operon promoter and regulation of hyaluronic acid capsule expression in group A Streptococcus
    • Alberti S, Ashbaugh CD, Wessels M. Structure of the has operon promoter and regulation of hyaluronic acid capsule expression in group A Streptococcus. Mol Microbiol 1998; 28: 343-53.
    • (1998) Mol Microbiol , vol.28 , pp. 343-353
    • Alberti, S.1    Ashbaugh, C.D.2    Wessels, M.3
  • 25
    • 0031656714 scopus 로고    scopus 로고
    • Molecular analysis of the capsule gene region of Group A Streptococcus: The has AB genes are sufficient for capsule expression
    • Ashbaugh CD, Alberti S, Wessels M. Molecular analysis of the capsule gene region of Group A Streptococcus: the has AB genes are sufficient for capsule expression. J Bacteriol 1998; 180: 4955-59.
    • (1998) J Bacteriol , vol.180 , pp. 4955-4959
    • Ashbaugh, C.D.1    Alberti, S.2    Wessels, M.3
  • 26
    • 0019429611 scopus 로고
    • Hyaluronate capsule prevents attachment of group A streptococci to mouse peritoneal macrophages
    • Whitnack E, Bisno AL, Beachey EH. Hyaluronate capsule prevents attachment of group A streptococci to mouse peritoneal macrophages. Infect Immun 1981; 31: 985-91.
    • (1981) Infect Immun , vol.31 , pp. 985-991
    • Whitnack, E.1    Bisno, A.L.2    Beachey, E.H.3
  • 28
    • 0344559090 scopus 로고
    • The role of mucoid hemolytic streptococci in rheumatic fever and arthritis
    • Pilot I. The role of mucoid hemolytic streptococci in rheumatic fever and arthritis. Proceedings of the Central Society for Clinical Research 1944; 17: 70-71.
    • (1944) Proceedings of the Central Society for Clinical Research , vol.17 , pp. 70-71
    • Pilot, I.1
  • 29
    • 0029897540 scopus 로고    scopus 로고
    • The nature of rheumatogenic streptococci
    • Stollerman GH. The nature of rheumatogenic streptococci. Mt Sinai J Med 1996; 63: 144-58.
    • (1996) Mt Sinai J Med , vol.63 , pp. 144-158
    • Stollerman, G.H.1
  • 30
    • 0026717164 scopus 로고
    • Epidemiologic analysis of group A streptococcal serotypes associated with severe systemic infections, rheumatic fever, or uncomplicated pharyngitis
    • Johnson DR, Stevens DL, Kaplan EL. Epidemiologic analysis of group A streptococcal serotypes associated with severe systemic infections, rheumatic fever, or uncomplicated pharyngitis. J Infect Dis 1992; 166: 374-82.
    • (1992) J Infect Dis , vol.166 , pp. 374-382
    • Johnson, D.R.1    Stevens, D.L.2    Kaplan, E.L.3
  • 31
    • 0022548959 scopus 로고
    • Induction of antibodies to hyaluronic acid by immunization of rabbits with encapsulated streptococci
    • Fillit HM, McCarty M, Blake M. Induction of antibodies to hyaluronic acid by immunization of rabbits with encapsulated streptococci. J Exp Med 1986; 164: 762-76.
    • (1986) J Exp Med , vol.164 , pp. 762-776
    • Fillit, H.M.1    McCarty, M.2    Blake, M.3
  • 32
    • 0023785825 scopus 로고
    • Immunogenicity of liposome-bound hyaluronate in mice: At least two different antigenic sites on hyaluronate are identified by mouse monoclonal antibodies
    • Fillit HM, Blake M, MacDonald C, McCarty M. Immunogenicity of liposome-bound hyaluronate in mice: at least two different antigenic sites on hyaluronate are identified by mouse monoclonal antibodies. J Exp Med 1988; 168: 971-82.
    • (1988) J Exp Med , vol.168 , pp. 971-982
    • Fillit, H.M.1    Blake, M.2    MacDonald, C.3    McCarty, M.4
  • 33
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham MW. Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 2000; 13: 470-511.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 34
    • 0036266507 scopus 로고    scopus 로고
    • Molecular mechanisms of adhesion, colonization, and invasion of group A streptococci
    • Courtney HS, Hasty DL, Dale JB. Molecular mechanisms of adhesion, colonization, and invasion of group A streptococci. Ann Med 2002; 34: 77-87.
    • (2002) Ann Med , vol.34 , pp. 77-87
    • Courtney, H.S.1    Hasty, D.L.2    Dale, J.B.3
  • 35
    • 0020049582 scopus 로고
    • The adherence of group A streptococci to oropharyngeal cells: The lipoteichoic acid adhesin and fibronectin receptor
    • Beachey EH, Simpson WA. The adherence of group A streptococci to oropharyngeal cells: the lipoteichoic acid adhesin and fibronectin receptor. Infection 1982; 10: 107-11.
    • (1982) Infection , vol.10 , pp. 107-111
    • Beachey, E.H.1    Simpson, W.A.2
  • 36
    • 0344127548 scopus 로고
    • Cell membrane-binding properties of group A streptococcal lipoteichoic acid
    • Ofek I, Beachey EH, Jefferson W, Campbell GL. Cell membrane-binding properties of group A streptococcal lipoteichoic acid. J Exp Med 1975; 187: 1161-67.
    • (1975) J Exp Med , vol.187 , pp. 1161-1167
    • Ofek, I.1    Beachey, E.H.2    Jefferson, W.3    Campbell, G.L.4
  • 37
    • 0028154087 scopus 로고
    • Passive protection of mice against group A streptococcal pharyngeal infection by lipoteichoic acid
    • Dale JB, Baird RW, Courtney HS, Hasty DL, Bronze MS. Passive protection of mice against group A streptococcal pharyngeal infection by lipoteichoic acid. J Infect Dis 1994; 169: 319-23.
    • (1994) J Infect Dis , vol.169 , pp. 319-323
    • Dale, J.B.1    Baird, R.W.2    Courtney, H.S.3    Hasty, D.L.4    Bronze, M.S.5
  • 39
    • 0015978213 scopus 로고
    • Parameters affecting the adherence and tissue tropisms of Streptococcus pyogenes
    • Ellen RP, Gibbons RJ. Parameters affecting the adherence and tissue tropisms of Streptococcus pyogenes. Inject Immun 1974; 9: 85-91.
    • (1974) Inject Immun , vol.9 , pp. 85-91
    • Ellen, R.P.1    Gibbons, R.J.2
  • 41
    • 0028089775 scopus 로고
    • Analysis of the role of M24 protein in group A streptococcal adhesion and colonization by use of omega-interposon mutagenesis
    • Courtney HS, Bronze MS, Dale JB, Hasty DL. Analysis of the role of M24 protein in group A streptococcal adhesion and colonization by use of omega-interposon mutagenesis. Infect Immun 1994; 62: 4868-73.
    • (1994) Infect Immun , vol.62 , pp. 4868-4873
    • Courtney, H.S.1    Bronze, M.S.2    Dale, J.B.3    Hasty, D.L.4
  • 42
    • 0027158446 scopus 로고
    • Role of M protein in pharyngeal colonization by group A streptococci in rats
    • Hollingshead SK, Simecka JW, Michalek SM. Role of M protein in pharyngeal colonization by group A streptococci in rats. Infect Immun 1993; 61: 2277-83.
    • (1993) Infect Immun , vol.61 , pp. 2277-2283
    • Hollingshead, S.K.1    Simecka, J.W.2    Michalek, S.M.3
  • 43
    • 0028008787 scopus 로고
    • M protein mediates streptococcal adhesion to HEp-2 cells
    • Wang JR, Stinson MW. M protein mediates streptococcal adhesion to HEp-2 cells. Infect Immun 1994; 62: 442-48.
    • (1994) Infect Immun , vol.62 , pp. 442-448
    • Wang, J.R.1    Stinson, M.W.2
  • 44
    • 0030976402 scopus 로고    scopus 로고
    • Conversion of M serotype 24 of Streptococcus pyogenes to M serotypes 5 and 18: Effect on resistance to phagocytosis and adhesion to host cells
    • Courtney HS, Liu S, Dale JB, Hasty DL. Conversion of M serotype 24 of Streptococcus pyogenes to M serotypes 5 and 18: effect on resistance to phagocytosis and adhesion to host cells. Infect Immun 1997; 65: 2472-74.
    • (1997) Infect Immun , vol.65 , pp. 2472-2474
    • Courtney, H.S.1    Liu, S.2    Dale, J.B.3    Hasty, D.L.4
  • 45
    • 0028023460 scopus 로고
    • M protein and protein F act as important determinants of cell-specific tropism of Streptococcuspyogenes in skin tissue
    • Okada N, Pentland AP, Falk P, Caparon MG. M protein and protein F act as important determinants of cell-specific tropism of Streptococcuspyogenes in skin tissue. J Clin Invest 1994; 94: 965-77.
    • (1994) J Clin Invest , vol.94 , pp. 965-977
    • Okada, N.1    Pentland, A.P.2    Falk, P.3    Caparon, M.G.4
  • 46
    • 0028935315 scopus 로고
    • Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus
    • Okada N, Liszewski MK, Atkinson JP, Caparon M. Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus. Proc Natl Acad Sci USA 1995; 92: 2489-93.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2489-2493
    • Okada, N.1    Liszewski, M.K.2    Atkinson, J.P.3    Caparon, M.4
  • 47
    • 0026661424 scopus 로고
    • Protein F, a fibronectinbinding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes
    • Hanski E, Caparon M. Protein F, a fibronectinbinding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes. Proc Natl Acad Sci USA 1992; 89: 6172-76.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6172-6176
    • Hanski, E.1    Caparon, M.2
  • 48
    • 0026706763 scopus 로고
    • Fihronectin-hinding 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. Fihronectin-hinding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun 1992; 60: 3837-44.
    • (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
  • 49
    • 0029130366 scopus 로고
    • Characterization of a novel fibronectin-binding surface protein in group A streptococci
    • Kreikemeyer B, Talay SR, Chhatwal GS. Characterization of a novel fibronectin-binding surface protein in group A streptococci. Mol Microbiol 1995; 17: 137-45.
    • (1995) Mol Microbiol , vol.17 , pp. 137-145
    • Kreikemeyer, B.1    Talay, S.R.2    Chhatwal, G.S.3
  • 50
    • 0029945894 scopus 로고    scopus 로고
    • Differential effects of the streptococcal fibronectin-binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and HEp-2 tissue culture cells
    • Courtney HS, Dale JB, Hasty DL. Differential effects of the streptococcal fibronectin-binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and HEp-2 tissue culture cells. Infect Immun 1996; 64: 2415-19.
    • (1996) Infect Immun , vol.64 , pp. 2415-2419
    • Courtney, H.S.1    Dale, J.B.2    Hasty, D.L.3
  • 51
    • 0029744998 scopus 로고    scopus 로고
    • Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains
    • Jaffe J, Natanson-Yaron S, Caparon MG, Hanski E. Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains. Mol Microbiol 1996; 21: 373-84.
    • (1996) Mol Microbiol , vol.21 , pp. 373-384
    • Jaffe, J.1    Natanson-Yaron, S.2    Caparon, M.G.3    Hanski, E.4
  • 52
    • 0032986477 scopus 로고    scopus 로고
    • Identification and characterization of a novel fibronectin-binding protein on the surface of group A streptococci
    • Rocha CL, Fischetti VA. Identification and characterization of a novel fibronectin-binding protein on the surface of group A streptococci. Infect Immun 1999; 67: 2720-28.
    • (1999) Infect Immun , vol.67 , pp. 2720-2728
    • Rocha, C.L.1    Fischetti, V.A.2
  • 53
    • 0026469139 scopus 로고
    • Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells
    • Hanski E, Horwitz PA, Caparon MG. Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect Immun 1992; 60: 5119-25.
    • (1992) Infect Immun , vol.60 , pp. 5119-5125
    • Hanski, E.1    Horwitz, P.A.2    Caparon, M.G.3
  • 54
    • 0032948058 scopus 로고    scopus 로고
    • Protective immune response against Streptococcus pyogenes in mice after intranasal vaccination with the fibronectin-binding protein SfbI
    • Guzman CA, Talay SR, Molinari G, Medina E, Chhatwal GS. Protective immune response against Streptococcus pyogenes in mice after intranasal vaccination with the fibronectin-binding protein SfbI. J Infect Dis 1999; 179: 901-6.
    • (1999) J Infect Dis , vol.179 , pp. 901-906
    • Guzman, C.A.1    Talay, S.R.2    Molinari, G.3    Medina, E.4    Chhatwal, G.S.5
  • 56
    • 0026808610 scopus 로고
    • Environmental regulation of virulence in group A streptococci: Transcription of the gene encoding M protein is stimulated by carbon dioxide
    • Caparon MG, Geist RT, Perez-Casal J, Scott JR. Environmental regulation of virulence in group A streptococci: transcription of the gene encoding M protein is stimulated by carbon dioxide. J Bacteriol 1992; 174: 5693-701.
    • (1992) J Bacteriol , vol.174 , pp. 5693-5701
    • Caparon, M.G.1    Geist, R.T.2    Perez-Casal, J.3    Scott, J.R.4
  • 58
    • 0033860082 scopus 로고    scopus 로고
    • Bacterial determinants of persistent throat colonization and the associated immune response in a primate model of human group A streptococcal pharyngeal infection
    • Ashbaugh CD, Moser TJ, Shearer MH, White GL, Kennedy RC, Wessels MR. Bacterial determinants of persistent throat colonization and the associated immune response in a primate model of human group A streptococcal pharyngeal infection. Cell Microbiol 2000; 2:283-92.
    • (2000) Cell Microbiol , vol.2 , pp. 283-292
    • Ashbaugh, C.D.1    Moser, T.J.2    Shearer, M.H.3    White, G.L.4    Kennedy, R.C.5    Wessels, M.R.6
  • 59
    • 0028109950 scopus 로고
    • Critical role of the group a streptococcal capsule in pharyngeal colonization and infection in mice
    • Wessels MR, Bronze MS. Critical role of the group a streptococcal capsule in pharyngeal colonization and infection in mice. Proc Natl Acad Sci USA 1994; 91: 12238-42.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12238-12242
    • Wessels, M.R.1    Bronze, M.S.2
  • 60
    • 0028046519 scopus 로고
    • Group A streptococci efficiently invade human respiratory epithelial cells
    • LaPenta D, Rubens C, Chi E, Cleary PP. Group A streptococci efficiently invade human respiratory epithelial cells. Proc Natl Acad Sci USA 1994; 91: 12115-19.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12115-12119
    • LaPenta, D.1    Rubens, C.2    Chi, E.3    Cleary, P.P.4
  • 61
    • 0031686023 scopus 로고    scopus 로고
    • Streptococcus pyogees serotype M 1 encodes multiple pathways for entry into human epithelial cells
    • Cue D, Dombek PE, Lam H, Cleary PP. Streptococcus pyogees serotype M 1 encodes multiple pathways for entry into human epithelial cells. Infect Immun 1998; 66: 4593-601.
    • (1998) Infect Immun , vol.66 , pp. 4593-4601
    • Cue, D.1    Dombek, P.E.2    Lam, H.3    Cleary, P.P.4
  • 62
    • 0033002358 scopus 로고    scopus 로고
    • Comparison of adherence to and penetration of a human laryngeal epithelial cell line by group A streptococci of various M protein types
    • Hagman MM, Dale JB, Stevens DL. Comparison of adherence to and penetration of a human laryngeal epithelial cell line by group A streptococci of various M protein types. FEMS Immunol Med Microbiol 1999; 23: 195-204.
    • (1999) FEMS Immunol Med Microbiol , vol.23 , pp. 195-204
    • Hagman, M.M.1    Dale, J.B.2    Stevens, D.L.3
  • 63
    • 0032904116 scopus 로고    scopus 로고
    • Highfrequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements
    • Dombek PE, Cue D, Sedgewick J, et al. Highfrequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements. Mol Microbiol 1999; 31: 859-70.
    • (1999) Mol Microbiol , vol.31 , pp. 859-870
    • Dombek, P.E.1    Cue, D.2    Sedgewick, J.3
  • 64
    • 0030903802 scopus 로고    scopus 로고
    • The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group ofgroup A streptococci by epithelial cells 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. The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group ofgroup A streptococci by epithelial cells The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect Immun 1997; 65: 1357-63.
    • (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
  • 65
    • 0031789927 scopus 로고    scopus 로고
    • Roles ofintegrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein Fl
    • Ozeri V, Rosenshine I, Mosher DF, Fassler R, Hanski E. Roles ofintegrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein Fl. Mol Microbiol 1998; 30: 625-37.
    • (1998) Mol Microbiol , vol.30 , pp. 625-637
    • Ozeri, V.1    Rosenshine, I.2    Mosher, D.F.3    Fassler, R.4    Hanski, E.5
  • 66
    • 0029120169 scopus 로고
    • Intracellular penetration and survival of Streptococcus pyogenes in respiratory epithelial cells in vitro
    • Osterlund A, Engstrand L. Intracellular penetration and survival of Streptococcus pyogenes in respiratory epithelial cells in vitro. Acta Otolaryngol 1995; 115: 685-88.
    • (1995) Acta Otolaryngol , vol.115 , pp. 685-688
    • Osterlund, A.1    Engstrand, L.2
  • 67
    • 0030667715 scopus 로고    scopus 로고
    • An intracellular sanctuary for Streptococcuspyogenes in human tonsillar epithelium - Studies of asymptomatic carriers and in vitro cultured biopsies
    • Osterlund A, Engstrand L. An intracellular sanctuary for Streptococcuspyogenes in human tonsillar epithelium - studies of asymptomatic carriers and in vitro cultured biopsies. Acta Otolaryngol 1997; 117: 883-88.
    • (1997) Acta Otolaryngol , vol.117 , pp. 883-888
    • Osterlund, A.1    Engstrand, L.2
  • 68
    • 0036155957 scopus 로고    scopus 로고
    • Role of CsrR, hyaluronic acid, and SpeB in the internalization of Streptococcus pyogenes M type 3 strain by epithelial cells
    • Jadoun J, Eyal O, Sela S. Role of CsrR, hyaluronic acid, and SpeB in the internalization of Streptococcus pyogenes M type 3 strain by epithelial cells. Infect Immun 2002; 70: 462-69.
    • (2002) Infect Immun , vol.70 , pp. 462-469
    • Jadoun, J.1    Eyal, O.2    Sela, S.3
  • 69
    • 0033982985 scopus 로고    scopus 로고
    • Role of group A streptococcal virulence factors in adherence to keratinocytes
    • Darmstadt GL, Mentele L, Podbielski A, Rubens CE. Role of group A streptococcal virulence factors in adherence to keratinocytes. Infect Immun 2000; 68: 1215-21.
    • (2000) Infect Immun , vol.68 , pp. 1215-1221
    • Darmstadt, G.L.1    Mentele, L.2    Podbielski, A.3    Rubens, C.E.4
  • 70
    • 0029957927 scopus 로고    scopus 로고
    • Hyaluronic acid capsule and the role of streptococcal entry into keratinocytes in invasive skin infection
    • Schrager HM, Rheinwald JG, Wessels MR. Hyaluronic acid capsule and the role of streptococcal entry into keratinocytes in invasive skin infection. J Clin Invest 1996; 98: 1954-58.
    • (1996) J Clin Invest , vol.98 , pp. 1954-1958
    • Schrager, H.M.1    Rheinwald, J.G.2    Wessels, M.R.3
  • 71
    • 0032145096 scopus 로고    scopus 로고
    • Molecular analysis of the role of the group a streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection
    • Ashbaugh CD, Warren HB, Carey VJ, Wessels MR. Molecular analysis of the role of the group a streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection. J Clin Invest 1998; 102: 550-60.
    • (1998) J Clin Invest , vol.102 , pp. 550-560
    • Ashbaugh, C.D.1    Warren, H.B.2    Carey, V.J.3    Wessels, M.R.4
  • 72
    • 0032523209 scopus 로고    scopus 로고
    • Hyaluronic acid capsule modulates M protein-mediated adherence and acts as a ligand for attachment of group A streptococcus to CD44 on human keratinocytes
    • Schrager HM, Alberti S, Cywes C, Dougherty GJ, Wessels MR. Hyaluronic acid capsule modulates M protein-mediated adherence and acts as a ligand for attachment of group A streptococcus to CD44 on human keratinocytes. J Clin Invest 1998; 101: 1708-16.
    • (1998) J Clin Invest , vol.101 , pp. 1708-1716
    • Schrager, H.M.1    Alberti, S.2    Cywes, C.3    Dougherty, G.J.4    Wessels, M.R.5
  • 73
    • 0033787963 scopus 로고    scopus 로고
    • CD44 as a receptor for colonization of the pharynx by group A Streptococcus
    • Cywes C, Stamenkovic I, Wessels MR. CD44 as a receptor for colonization of the pharynx by group A Streptococcus. J Clin Invest 2000; 106: 995-1002.
    • (2000) J Clin Invest , vol.106 , pp. 995-1002
    • Cywes, C.1    Stamenkovic, I.2    Wessels, M.R.3
  • 74
    • 0035818973 scopus 로고    scopus 로고
    • Group A streptococcus tissue invasion by CD44-mediated cell signalling
    • Cywes C, Wessels MR. Group A streptococcus tissue invasion by CD44-mediated cell signalling. Nature 2001; 414: 648-52.
    • (2001) Nature , vol.414 , pp. 648-652
    • Cywes, C.1    Wessels, M.R.2
  • 75
    • 0035846909 scopus 로고    scopus 로고
    • Cytolysin-mediated translocation (CMT): A functional equivalent of type III secretion in gram-positive bacteria
    • Madden JC, Ruiz N, Caparon M. Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in gram-positive bacteria. Cell 2001; 104: 143-52.
    • (2001) Cell , vol.104 , pp. 143-152
    • Madden, J.C.1    Ruiz, N.2    Caparon, M.3
  • 76
    • 0036129905 scopus 로고    scopus 로고
    • Antibodies against a synthetic peptide of Saga neutralize the cytolytic activity of streptolysin S from group A streptococci
    • Dale JB, Chiang EY, Hasty DL, Courtney HS. Antibodies against a synthetic peptide of Saga neutralize the cytolytic activity of streptolysin S from group A streptococci. Infect Immun 2002; 70: 2166-70.
    • (2002) Infect Immun , vol.70 , pp. 2166-2170
    • Dale, J.B.1    Chiang, E.Y.2    Hasty, D.L.3    Courtney, H.S.4
  • 77
    • 0035834742 scopus 로고    scopus 로고
    • Similarities between complement-mediated and streptolysin S-mediated hemolysis
    • Carr A, Sledjeski DD, Podbielski A, Boyle MD, Kreikemeyer B. Similarities between complement-mediated and streptolysin S-mediated hemolysis. J Biol Chem 2001; 276: 41790-96.
    • (2001) J Biol Chem , vol.276 , pp. 41790-41796
    • Carr, A.1    Sledjeski, D.D.2    Podbielski, A.3    Boyle, M.D.4    Kreikemeyer, B.5
  • 78
    • 9044220226 scopus 로고    scopus 로고
    • C5a peptidase alters clearance and trafficking of group A streptococci by infected mice
    • Yinduo J, McLandshorough L, Kondagunta A, Cleary PP. C5a peptidase alters clearance and trafficking of group A streptococci by infected mice. Infect Immun 1996; 64: 503-10.
    • (1996) Infect Immun , vol.64 , pp. 503-510
    • Yinduo, J.1    McLandshorough, L.2    Kondagunta, A.3    Cleary, P.P.4
  • 79
    • 0022406656 scopus 로고
    • Mechanism of action of the group A streptococcal C5a inactivator
    • Wexler DE, Chenoweth DE, Cleary PP. Mechanism of action of the group A streptococcal C5a inactivator. Proc Natl Acad Sci USA 1985; 82: 8144-48.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8144-8148
    • Wexler, D.E.1    Chenoweth, D.E.2    Cleary, P.P.3
  • 80
    • 0036716438 scopus 로고    scopus 로고
    • Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: Secretory leukocyte proteinase inhibitor and lysozyme
    • Fernie-King BA, Seilly DJ, Davies A, Lachmann PJ. Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: secretory leukocyte proteinase inhibitor and lysozyme. Infect Immun 2002; 70: 4908-16.
    • (2002) Infect Immun , vol.70 , pp. 4908-4916
    • Fernie-King, B.A.1    Seilly, D.J.2    Davies, A.3    Lachmann, P.J.4
  • 81
    • 0034937066 scopus 로고    scopus 로고
    • Streptococcal inhibitor of complement (SIC) inhibits the membrane attack complex by preventing uptake of C567 onto cell membranes
    • Fernie-King BA, Seilly DJ, Willers C, Wurzner R, Davies A, Lachmann PJ. Streptococcal inhibitor of complement (SIC) inhibits the membrane attack complex by preventing uptake of C567 onto cell membranes. Immunology 2001; 103: 390-98.
    • (2001) Immunology , vol.103 , pp. 390-398
    • Fernie-King, B.A.1    Seilly, D.J.2    Willers, C.3    Wurzner, R.4    Davies, A.5    Lachmann, P.J.6
  • 82
    • 0037188512 scopus 로고    scopus 로고
    • Insight into the molecular basis of pathogen abundance: Group A streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells
    • Hoe NP, Ireland RM, DeLeo FR, et al. Insight into the molecular basis of pathogen abundance: group A streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells. Proc Natl Acad Sci USA 2002; 99: 7646-51.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7646-7651
    • Hoe, N.P.1    Ireland, R.M.2    DeLeo, F.R.3
  • 83
    • 0035006360 scopus 로고    scopus 로고
    • Structural features of a zinc binding site in the superantigen strepococcal pyrogenic exotoxin A (SpcA1): Implications for MHC class II recognition
    • Baker M, Gutman DM, Papageorgiou AC, Collins CM, Acharya KR. Structural features of a zinc binding site in the superantigen strepococcal pyrogenic exotoxin A (SpcA1): implications for MHC class II recognition. Protein Sci 2001; 10: 1268-73.
    • (2001) Protein Sci , vol.10 , pp. 1268-1273
    • Baker, M.1    Gutman, D.M.2    Papageorgiou, A.C.3    Collins, C.M.4    Acharya, K.R.5
  • 84
    • 0036721611 scopus 로고    scopus 로고
    • The bacterial superantigen streptococcal mitogenic exotoxin Z is the major immunoactive agent of Streptococcus pyogenes
    • Unnikrishnan M, Altmann DM, Proft T, et al. The bacterial superantigen streptococcal mitogenic exotoxin Z is the major immunoactive agent of Streptococcus pyogenes. J Immunol 2002; 169: 2561-69.
    • (2002) J Immunol , vol.169 , pp. 2561-2569
    • Unnikrishnan, M.1    Altmann, D.M.2    Proft, T.3
  • 85
    • 0036892190 scopus 로고    scopus 로고
    • Characterization of two novel pyrogenic toxin superantigens made by an acute rheumatic fever clone of Streptococcus pyogenes associated with multiple disease outbreaks
    • Smoot LM, McCormick JK, Smoot JC, et al. Characterization of two novel pyrogenic toxin superantigens made by an acute rheumatic fever clone of Streptococcus pyogenes associated with multiple disease outbreaks. Infect Immun 2002; 70: 7095-104.
    • (2002) Infect Immun , vol.70 , pp. 7095-7104
    • Smoot, L.M.1    McCormick, J.K.2    Smoot, J.C.3
  • 86
    • 0033521685 scopus 로고    scopus 로고
    • Structural basis for the recognition ofsuperantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors
    • Papageorgiou AC, Collins CM, Gutman DM, et al. Structural basis for the recognition ofsuperantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors. EMBO J 1999; 18: 9-21.
    • (1999) EMBO J , vol.18 , pp. 9-21
    • Papageorgiou, A.C.1    Collins, C.M.2    Gutman, D.M.3
  • 87
    • 0030798632 scopus 로고    scopus 로고
    • Crystal structure of the streptococcal superantigen Spe C: Dimerization and zinc-binding suggest a novel mode of interaction with MHC class II molecules
    • Roussell A, Anderson BF, Baker HM, Fraser JD, Baker EN. Crystal structure of the streptococcal superantigen Spe C: dimerization and zinc-binding suggest a novel mode of interaction with MHC class II molecules. Nat Struct Biol 2002; 4: 635-43.
    • (2002) Nat Struct Biol , vol.4 , pp. 635-643
    • Roussell, A.1    Anderson, B.F.2    Baker, H.M.3    Fraser, J.D.4    Baker, E.N.5
  • 88
    • 0034716945 scopus 로고    scopus 로고
    • Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes
    • Arcus VL, Proft T, Sigrell JA, Baker HM, Fraser JD, Baker EN. Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes. J Mol Biol 2000; 299: 157-68.
    • (2000) J Mol Biol , vol.299 , pp. 157-168
    • Arcus, V.L.1    Proft, T.2    Sigrell, J.A.3    Baker, H.M.4    Fraser, J.D.5    Baker, E.N.6
  • 89
    • 0034254854 scopus 로고    scopus 로고
    • Microbial superantigens: From structure to function
    • Papageorgiou AC, Acharya KR. Microbial superantigens: from structure to function. Trends Microbiol 2000; 8: 369-75.
    • (2000) Trends Microbiol , vol.8 , pp. 369-375
    • Papageorgiou, A.C.1    Acharya, K.R.2
  • 90
    • 37049178741 scopus 로고
    • The staphylococcal enterotoxins and their relatives
    • Marrack P, Kappler J. The staphylococcal enterotoxins and their relatives. Science 1990; 248: 705-11.
    • (1990) Science , vol.248 , pp. 705-711
    • Marrack, P.1    Kappler, J.2
  • 91
    • 0031669859 scopus 로고    scopus 로고
    • Toxin-mediated streptococcal and staphylococcal disease
    • Manders SM. Toxin-mediated streptococcal and staphylococcal disease. J Am Acad Dermatol 1999; 39: 383-98.
    • (1999) J Am Acad Dermatol , vol.39 , pp. 383-398
    • Manders, S.M.1
  • 92
    • 0025044872 scopus 로고
    • Staphylococcal and streptococcal pyrogenic toxins involved in toxic shock syndrome and related illnesses
    • Bohach GA, Fast DJ, Nelson RD, Schlievert PM. Staphylococcal and streptococcal pyrogenic toxins involved in toxic shock syndrome and related illnesses. CRC Crit Rev Microbiol 1990; 17: 251-72.
    • (1990) CRC Crit Rev Microbiol , vol.17 , pp. 251-272
    • Bohach, G.A.1    Fast, D.J.2    Nelson, R.D.3    Schlievert, P.M.4
  • 93
    • 0025894808 scopus 로고
    • Molecular analysis of pyrogenic exotoxins from Streptococcus pyogenes isolates associated with toxic shock-like syndrome
    • Hauser AR, Stevens DL, Kaplan EL, Schlievert PM. Molecular analysis of pyrogenic exotoxins from Streptococcus pyogenes isolates associated with toxic shock-like syndrome. J Clin Microbiol 1991; 29: 1562-67.
    • (1991) J Clin Microbiol , vol.29 , pp. 1562-1567
    • Hauser, A.R.1    Stevens, D.L.2    Kaplan, E.L.3    Schlievert, P.M.4
  • 94
    • 0034773523 scopus 로고    scopus 로고
    • Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins
    • Collin M, Olsen A. Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins. Infect Immun 2001; 69: 7187-89.
    • (2001) Infect Immun , vol.69 , pp. 7187-7189
    • Collin, M.1    Olsen, A.2
  • 95
    • 0027290733 scopus 로고
    • Cleavage ofinterleukin Ibeta (IL-1beta) precursor to produce active IL-lbeta by a conserved extracellular cysteine protease from Streptococcus pyogenes
    • Kapur V, Majesky MW, Li LL, Black RA, Musser JM. Cleavage ofinterleukin Ibeta (IL-1beta) precursor to produce active IL-lbeta by a conserved extracellular cysteine protease from Streptococcus pyogenes. Proc Natl Acad Sci USA 1993; 90: 7676-80.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7676-7680
    • Kapur, V.1    Majesky, M.W.2    Li, L.L.3    Black, R.A.4    Musser, J.M.5
  • 96
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism
    • Herwald H, Collin M, Muller-Esterl W, Bjorck L. Streptococcal cysteine proteinase releases kinins: a novel virulence mechanism. J Exp Med 1996; 184: 665-73.
    • (1996) J Exp Med , vol.184 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Muller-Esterl, W.3    Bjorck, L.4
  • 97
    • 0036084422 scopus 로고    scopus 로고
    • Cysteine protease activity and histamine release from the uman mast cell line HMC-1 stimulated by recombinant streptococcal pyrogenic exotoxin B/streptococcal cysteine protease
    • Watanabe Y, Todome Y, Ohkuni H, et al. Cysteine protease activity and histamine release from the uman mast cell line HMC-1 stimulated by recombinant streptococcal pyrogenic exotoxin B/streptococcal cysteine protease. Infect Immun 2002; 70: 3944-47.
    • (2002) Infect Immun , vol.70 , pp. 3944-3947
    • Watanabe, Y.1    Todome, Y.2    Ohkuni, H.3
  • 98
    • 0031906945 scopus 로고    scopus 로고
    • Genetic inactivation of an extracellular cysteine protease (SpeB) expressed by Streptococcus pyogenes decreases resistance to phagocytosis and dissemination to organs
    • Lukomski S, Burns EHJ, Wyde PR, et al. Genetic inactivation of an extracellular cysteine protease (SpeB) expressed by Streptococcus pyogenes decreases resistance to phagocytosis and dissemination to organs. Infect Immun 1998; 66: 771-76.
    • (1998) Infect Immun , vol.66 , pp. 771-776
    • Lukomski, S.1    Burns, E.H.J.2    Wyde, P.R.3
  • 99
    • 0035884264 scopus 로고    scopus 로고
    • Streptococcal pyrogenic exotoxin B enhances tissue damage initiated by other Streptococcus pyogenes products
    • Saouda M, Wu W, Conran P, Boyle MD. Streptococcal pyrogenic exotoxin B enhances tissue damage initiated by other Streptococcus pyogenes products. J Infect Dis 2001; 184: 723-31.
    • (2001) J Infect Dis , vol.184 , pp. 723-731
    • Saouda, M.1    Wu, W.2    Conran, P.3    Boyle, M.D.4
  • 100
    • 0031870998 scopus 로고    scopus 로고
    • Role of streptococcal pyrogenic exotoxin B in the mouse model of group A streptococcal infection
    • Kuo CF, Wu JJ, Lin KY, et al. Role of streptococcal pyrogenic exotoxin B in the mouse model of group A streptococcal infection. Infect Immun 1998; 66: 3931-35.
    • (1998) Infect Immun , vol.66 , pp. 3931-3935
    • Kuo, C.F.1    Wu, J.J.2    Lin, K.Y.3
  • 101
    • 0033791996 scopus 로고    scopus 로고
    • Inverse relation between disease severity and expression of the streptococcal cysteine protease, SpeB, among clonal M1T1 isolates recovered from invasive group A streptococcal infection cases
    • Kansal RG, McGeer A, Low DE, Norrby-Teglund A, Kotb M. Inverse relation between disease severity and expression of the streptococcal cysteine protease, SpeB, among clonal M1T1 isolates recovered from invasive group A streptococcal infection cases. Infect Immun 2000; 68: 6362-69.
    • (2000) Infect Immun , vol.68 , pp. 6362-6369
    • Kansal, R.G.1    McGeer, A.2    Low, D.E.3    Norrby-Teglund, A.4    Kotb, M.5
  • 102
    • 0036271592 scopus 로고    scopus 로고
    • Proteolysis and its regulation at the surface of Streptococcus pyogenes
    • Rasmussen M, Bjorck L. Proteolysis and its regulation at the surface of Streptococcus pyogenes. Mol Microbiol 2002; 43: 537-44.
    • (2002) Mol Microbiol , vol.43 , pp. 537-544
    • Rasmussen, M.1    Bjorck, L.2
  • 104
    • 0026596550 scopus 로고
    • Streptococcal toxic shock syndrome: Synthesis of tumor necrosis factor and interleukin-1 by monocytes stimulated with pyrogenic exotoxin A and streptolysin O
    • Hackett SP, Stevens DL. Streptococcal toxic shock syndrome: synthesis of tumor necrosis factor and interleukin-1 by monocytes stimulated with pyrogenic exotoxin A and streptolysin O. J Infect Dis 1992; 165: 879-85.
    • (1992) J Infect Dis , vol.165 , pp. 879-885
    • Hackett, S.P.1    Stevens, D.L.2
  • 105
    • 0033035861 scopus 로고    scopus 로고
    • Gram-positive sepsis. Mechanisms and differences from gram-negative sepsis
    • Sriskandan S, Cohen J. Gram-positive sepsis. Mechanisms and differences from gram-negative sepsis. Infect Dis Clin North Am 1999; 13: 397-412.
    • (1999) Infect Dis Clin North Am , vol.13 , pp. 397-412
    • Sriskandan, S.1    Cohen, J.2
  • 106
    • 0033040119 scopus 로고    scopus 로고
    • Risk factors in the pathogenesis of invasive group A streptococcal infections: Role of protective humoral immunity
    • Basma H, Norrby-Teglund A, Guedez Y, et al. Risk factors in the pathogenesis of invasive group A streptococcal infections: role of protective humoral immunity. Infect Immun 1999; 67: 1871-77.
    • (1999) Infect Immun , vol.67 , pp. 1871-1877
    • Basma, H.1    Norrby-Teglund, A.2    Guedez, Y.3
  • 107
    • 0033738808 scopus 로고    scopus 로고
    • Host variation in cytokine responses to superantigens determine the severity of invasive group A streptococcal infection
    • Norrby-Teglund A, Chatellier S, Low DE, McGeer A, Green K, Kotb M. Host variation in cytokine responses to superantigens determine the severity of invasive group A streptococcal infection. Eur J Immunol 2000; 30: 3247-55.
    • (2000) Eur J Immunol , vol.30 , pp. 3247-3255
    • Norrby-Teglund, A.1    Chatellier, S.2    Low, D.E.3    McGeer, A.4    Green, K.5    Kotb, M.6
  • 108
    • 0036908653 scopus 로고    scopus 로고
    • An immunogenetic and molecular basis for differences in outcomes of invasive group A streptococcal infections
    • Kotb M, Norrby-Teglund A, McGeer A, et al. An immunogenetic and molecular basis for differences in outcomes of invasive group A streptococcal infections. Nat Med 2002; 8:1398-404.
    • (2002) Nat Med , vol.8 , pp. 1398-1404
    • Kotb, M.1    Norrby-Teglund, A.2    McGeer, A.3
  • 109
    • 0035836659 scopus 로고    scopus 로고
    • Complete genome sequence of an M1 strain of Streptococcus pyogenes 1
    • Ferretti JJ, McShan WM, Ajdic D, et al. Complete genome sequence of an M1 strain of Streptococcus pyogenes 1. Proc Natl Acad Sci USA 2001; 98: 4658-63.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4658-4663
    • Ferretti, J.J.1    McShan, W.M.2    Ajdic, D.3
  • 110
    • 0037162559 scopus 로고    scopus 로고
    • Genome sequence ofa serotype M3 strain of group A streptococcus: Phage-encoded toxins, the high-virulence phenotype, and clone emergence
    • Beres SB, Sylva GL, Barbian KD, et al. Genome sequence ofa serotype M3 strain of group A streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence. Proc Natl Acad Sci USA 2002; 99: 10078-83.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10078-10083
    • Beres, S.B.1    Sylva, G.L.2    Barbian, K.D.3
  • 111
    • 0037007095 scopus 로고    scopus 로고
    • Genome sequence and comparative microarray analysis ofserotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks
    • Smoot JC, Barbian KD, Van Gompel JJ, et al. Genome sequence and comparative microarray analysis ofserotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks. Proc Natl Acad Sci USA 2002; 99: 4668-73.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4668-4673
    • Smoot, J.C.1    Barbian, K.D.2    Van Gompel, J.J.3
  • 112
    • 0036070576 scopus 로고    scopus 로고
    • Bacteriophage control of bacterial virulence
    • Wagner PL, Waldor MK. Bacteriophage control of bacterial virulence. Infect Immun 2002; 70: 3985-93.
    • (2002) Infect Immun , vol.70 , pp. 3985-3993
    • Wagner, P.L.1    Waldor, M.K.2
  • 113
    • 0025865798 scopus 로고
    • Mry, a transacting positive regulator of the M protein gene of Streprococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems
    • Perez-Casal J, Caparon MG, Scott JR. Mry, a transacting positive regulator of the M protein gene of Streprococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems. J Bacteriol 1991; 173: 2617-24.
    • (1991) J Bacteriol , vol.173 , pp. 2617-2624
    • Perez-Casal, J.1    Caparon, M.G.2    Scott, J.R.3
  • 114
    • 0031669931 scopus 로고    scopus 로고
    • Identification of csrR/csrS, a genetic locus that regulates hyaluronic acid capsule synthesis in group A Streptococcus
    • Levin JC, Wessels MR. Identification of csrR/csrS, a genetic locus that regulates hyaluronic acid capsule synthesis in group A Streptococcus. Mol Microbiol 1998; 30: 209-19.
    • (1998) Mol Microbiol , vol.30 , pp. 209-219
    • Levin, J.C.1    Wessels, M.R.2
  • 115
    • 0033053646 scopus 로고    scopus 로고
    • A response regulator that represses transcription of several virulence operons in the group A streptococcus
    • Federle MJ, McIver KS, Scott JR. A response regulator that represses transcription of several virulence operons in the group A streptococcus. J Bacteriol 1999; 181: 3649-57.
    • (1999) J Bacteriol , vol.181 , pp. 3649-3657
    • Federle, M.J.1    McIver, K.S.2    Scott, J.R.3
  • 116
    • 0032856769 scopus 로고    scopus 로고
    • A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B
    • Heath A, DiRita VJ, Barg NL, Engleberg NC. A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B. Infect Immun 1999; 67: 5298-305.
    • (1999) Infect Immun , vol.67 , pp. 5298-5305
    • Heath, A.1    DiRita, V.J.2    Barg, N.L.3    Engleberg, N.C.4
  • 117
    • 0027413670 scopus 로고
    • Positive transcriptional control of mry regulates virulence in the group A streptococcus
    • Okada N, Geist RT, Caparon MG. Positive transcriptional control of mry regulates virulence in the group A streptococcus. Mol Microbiol 1993; 7: 893-903.
    • (1993) Mol Microbiol , vol.7 , pp. 893-903
    • Okada, N.1    Geist, R.T.2    Caparon, M.G.3
  • 118
    • 0036267873 scopus 로고    scopus 로고
    • Two DNA-binding domains of Mga are required for virulence gene
    • McIver KS, Myles RL. Two DNA-binding domains of Mga are required for virulence gene. Mol Microbiol 2002; 43: 1591-601.
    • (2002) Mol Microbiol , vol.43 , pp. 1591-1601
    • McIver, K.S.1    Myles, R.L.2
  • 119
    • 0027423484 scopus 로고
    • Adherence and fibrinectin binding are environmentally regulated in the group A streptococci
    • Van Heyningen T, Fogg G, Yates D, Hanski E, Caparon M. Adherence and fibrinectin binding are environmentally regulated in the group A streptococci. Mol Microbiol 1993; 9: 1213-22.
    • (1993) Mol Microbiol , vol.9 , pp. 1213-1222
    • Van Heyningen, T.1    Fogg, G.2    Yates, D.3    Hanski, E.4    Caparon, M.5
  • 120
    • 0028237244 scopus 로고
    • The identification of rofA, a positive-acting regulatory component of prtF expression: Use of an m-gamma-delta-based shuttle mutagenesis strategy in Streptococcus pyogenes
    • Fogg GC, Gibson CM, Caparon MG. The identification of rofA, a positive-acting regulatory component of prtF expression: use of an m-gamma-delta-based shuttle mutagenesis strategy in Streptococcus pyogenes. Mol Microbiol 1994; 11: 671-84.
    • (1994) Mol Microbiol , vol.11 , pp. 671-684
    • Fogg, G.C.1    Gibson, C.M.2    Caparon, M.G.3
  • 121
    • 0033039873 scopus 로고    scopus 로고
    • Characterization of nra, a global negative regulator gene in group A streptococci
    • Podbielski A, Woischnik M, Leonard BA, Schmidt KH. Characterization of nra, a global negative regulator gene in group A streptococci. Mol Microbiol 1999; 31: 1051-64.
    • (1999) Mol Microbiol , vol.31 , pp. 1051-1064
    • Podbielski, A.1    Woischnik, M.2    Leonard, B.A.3    Schmidt, K.H.4
  • 122
    • 0034995382 scopus 로고    scopus 로고
    • Repression of virulence genes by phosphorylation-dependent oligomerization of CsrR at target promoters in S pyogenes
    • Miller AA, Engleberg NC, DiRita VJ. Repression of virulence genes by phosphorylation-dependent oligomerization of CsrR at target promoters in S pyogenes. Mol Microbiol 2001; 40:976-90.
    • (2001) Mol Microbiol , vol.40 , pp. 976-990
    • Miller, A.A.1    Engleberg, N.C.2    DiRita, V.J.3
  • 123
    • 0036229494 scopus 로고    scopus 로고
    • Identification of binding sites for the group A streptococcal global regulator CovR
    • Federle MJ, Scott JR. Identification of binding sites for the group A streptococcal global regulator CovR. Mol Microbiol 2002; 43: 1161-72.
    • (2002) Mol Microbiol , vol.43 , pp. 1161-1172
    • Federle, M.J.1    Scott, J.R.2
  • 124
    • 0037108912 scopus 로고    scopus 로고
    • Virulence control in group A streptococcus by a two-component gene regulatory system: Global expression profiling and in vivo infection modeling
    • Graham MR, Smoot LM, Migliaccio CA, et al. Virulence control in group A streptococcus by a two-component gene regulatory system: global expression profiling and in vivo infection modeling. Proc Natl Acad Sci USA 2002; 99: 13855-60.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13855-13860
    • Graham, M.R.1    Smoot, L.M.2    Migliaccio, C.A.3
  • 125
    • 0036153610 scopus 로고    scopus 로고
    • Rgg influences the expression of multiple regulatory loci to coregulate virulence factor expression in Streptococcus pyogenes
    • Chaussee MS, Sylva GL, Sturdevant DE, et al. Rgg influences the expression of multiple regulatory loci to coregulate virulence factor expression in Streptococcus pyogenes. Infect Immun 2002; 70: 762-70.
    • (2002) Infect Immun , vol.70 , pp. 762-770
    • Chaussee, M.S.1    Sylva, G.L.2    Sturdevant, D.E.3
  • 126
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon WR, Gibson CM, Caparon MG. A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J 1998; 17: 6263-75.
    • (1998) EMBO J , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 127
    • 0035151016 scopus 로고    scopus 로고
    • Group A streptococcal growth phase-associated virulence factor regulation by a novel operon (Fas) with homologies to two-component-type regulators requires a small RNA molecule
    • Kreikemeyer B, Boyle MD, Buttaro BA, Heinemann M, Podbielski A. Group A streptococcal growth phase-associated virulence factor regulation by a novel operon (Fas) with homologies to two-component-type regulators requires a small RNA molecule. Mol Microbiol 2001; 39: 392-406.
    • (2001) Mol Microbiol , vol.39 , pp. 392-406
    • Kreikemeyer, B.1    Boyle, M.D.2    Buttaro, B.A.3    Heinemann, M.4    Podbielski, A.5
  • 128
    • 0032822538 scopus 로고    scopus 로고
    • Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins
    • Li Z, Sledjeski DD, Kreikemeyer B, Podbielski A, Boyle MD. Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins. J Bacteriol 1999; 181: 6019-27.
    • (1999) J Bacteriol , vol.181 , pp. 6019-6027
    • Li, Z.1    Sledjeski, D.D.2    Kreikemeyer, B.3    Podbielski, A.4    Boyle, M.D.5
  • 130
    • 0035884736 scopus 로고    scopus 로고
    • Rheumatic fever in the 21st century
    • Stollerman GH. Rheumatic fever in the 21st century. Clin Infect Dis 2001; 33: 806-14.
    • (2001) Clin Infect Dis , vol.33 , pp. 806-814
    • Stollerman, G.H.1
  • 131
    • 0002770364 scopus 로고
    • The concept of rheumatogenic and non-rheumatogenic group A streptococci
    • Read SE, Zabriskie JB, eds. New York: Academic Press
    • Bisno AL. The concept of rheumatogenic and non-rheumatogenic group A streptococci. In: Read SE, Zabriskie JB, eds. Streptococcal diseases and the immune response. New York: Academic Press; 1980: 789-803.
    • (1980) Streptococcal Diseases and the Immune Response , pp. 789-803
    • Bisno, A.L.1
  • 132
    • 0036251948 scopus 로고    scopus 로고
    • Molecular analysis of group A Streptococcus type emm18 isolates temporally associated with acute rheumatic fever outbreaks in Salt Lake City, Utah
    • Smoot JC, Korgenski EK, Daly JA, Veasy LG, Musser JM. Molecular analysis of group A Streptococcus type emm18 isolates temporally associated with acute rheumatic fever outbreaks in Salt Lake City, Utah. J Clin Microbiol 2002; 40: 1805-10.
    • (2002) J Clin Microbiol , vol.40 , pp. 1805-1810
    • Smoot, J.C.1    Korgenski, E.K.2    Daly, J.A.3    Veasy, L.G.4    Musser, J.M.5
  • 133
    • 0025687903 scopus 로고
    • Differentiation between two biologically distinct classes of group A streptococci by limited substitutions of amino acids within the shared region of M protein-like molecules
    • Bessen DE, Fischetti VA. Differentiation between two biologically distinct classes of group A streptococci by limited substitutions of amino acids within the shared region of M protein-like molecules. J Exp Med 1990; 172: 1757-64.
    • (1990) J Exp Med , vol.172 , pp. 1757-1764
    • Bessen, D.E.1    Fischetti, V.A.2
  • 134
    • 0028791327 scopus 로고
    • Serologic evidence for a class I group A streptococcal infection among rheumatic fever patients
    • Bessen DE, Veasy LG, Hill HR, Augustine NH, Fischetti VA. Serologic evidence for a class I group A streptococcal infection among rheumatic fever patients. J Infect Dis 1995; 172: 1608-11.
    • (1995) J Infect Dis , vol.172 , pp. 1608-1611
    • Bessen, D.E.1    Veasy, L.G.2    Hill, H.R.3    Augustine, N.H.4    Fischetti, V.A.5
  • 135
    • 0020540072 scopus 로고
    • Nephritis caused by Streptococcus zooepidemicus (Lancefield group C)
    • Barnham M, Thornton TJ, Lange K. Nephritis caused by Streptococcus zooepidemicus (Lancefield group C). Lancet 1983; 1: 945-48.
    • (1983) Lancet , vol.1 , pp. 945-948
    • Barnham, M.1    Thornton, T.J.2    Lange, K.3
  • 136
    • 0014611093 scopus 로고
    • Chemistry of cross-reactive fragments of streptococcal cell membrane and human glomerular basement membrane
    • Lange CF. Chemistry of cross-reactive fragments of streptococcal cell membrane and human glomerular basement membrane. Transplant Proc 1969; 1: 959-63.
    • (1969) Transplant Proc , vol.1 , pp. 959-963
    • Lange, C.F.1
  • 137
    • 0023274353 scopus 로고
    • Monoclonal antibody to human renal glomeruli cross-reacts with streptococcal M protein
    • Goroncy-Bermes P, Dale JB, Beachey EH, Opferkuch W. Monoclonal antibody to human renal glomeruli cross-reacts with streptococcal M protein. Infect Immun 1987; 55: 2416-19.
    • (1987) Infect Immun , vol.55 , pp. 2416-2419
    • Goroncy-Bermes, P.1    Dale, J.B.2    Beachey, E.H.3    Opferkuch, W.4
  • 138
    • 0014686978 scopus 로고
    • Elution of glomerular bound antibodies in experimental streptococcal glomerulonephritis
    • Lindberg LH, Vosti KL. Elution of glomerular bound antibodies in experimental streptococcal glomerulonephritis. Science 1969; 166: 1032-33.
    • (1969) Science , vol.166 , pp. 1032-1033
    • Lindberg, L.H.1    Vosti, K.L.2
  • 139
    • 0015104328 scopus 로고
    • Streptococcal related glomerulonephritis 3. Glomerulonephritis in rhesus monkeys immunologically induced both actively and passively with a soluble fraction from nephritogenic streptococcal protoplasmic membranes
    • Markowitz AS, Horn D, Aseron C, Novak R, Battiforia HA. Streptococcal related glomerulonephritis 3. Glomerulonephritis in rhesus monkeys immunologically induced both actively and passively with a soluble fraction from nephritogenic streptococcal protoplasmic membranes. J Immunol 1971; 107: 504-11.
    • (1971) J Immunol , vol.107 , pp. 504-511
    • Markowitz, A.S.1    Horn, D.2    Aseron, C.3    Novak, R.4    Battiforia, H.A.5
  • 140
    • 0031684402 scopus 로고    scopus 로고
    • Immunohistochemical and serological evidence for the role of Streptococcal proteinase in acute post-streptococcal glomerulonephritis
    • Cu GA, Mezzano S, Bannan JD, Zabriskie JB. Immunohistochemical and serological evidence for the role of Streptococcal proteinase in acute post-streptococcal glomerulonephritis. Kidney Int 1999; 54: 819-26.
    • (1999) Kidney Int , vol.54 , pp. 819-826
    • Cu, G.A.1    Mezzano, S.2    Bannan, J.D.3    Zabriskie, J.B.4
  • 141
    • 0017156286 scopus 로고
    • A hitherto unknown streptococcal antigen and its probable relation to acute poststreptococcal glomerulonephritis
    • Lange K, Ahmed U, Kleinberger H, Treser G. A hitherto unknown streptococcal antigen and its probable relation to acute poststreptococcal glomerulonephritis. Clin Nephrol 1976; 5: 207-15.
    • (1976) Clin Nephrol , vol.5 , pp. 207-215
    • Lange, K.1    Ahmed, U.2    Kleinberger, H.3    Treser, G.4
  • 142
    • 0026523210 scopus 로고
    • Role of a streptococcal antigen in the pathogenesis of acute poststreptococcal glomerulonephritis
    • Yoshizawa N, Oshima S, Sagel I, Shimizu J, Treser G. Role of a streptococcal antigen in the pathogenesis of acute poststreptococcal glomerulonephritis. J Immunol 1992; 148: 3110-16.
    • (1992) J Immunol , vol.148 , pp. 3110-3116
    • Yoshizawa, N.1    Oshima, S.2    Sagel, I.3    Shimizu, J.4    Treser, G.5
  • 143
    • 0022589315 scopus 로고
    • Purification and partial characterization of the nephritis strain-associated protein from Streptococcuspyogenes, group A
    • Johnson KH, Zabriskie JB. Purification and partial characterization of the nephritis strain-associated protein from Streptococcuspyogenes, group A. J Exp Med 1986; 163: 697-712.
    • (1986) J Exp Med , vol.163 , pp. 697-712
    • Johnson, K.H.1    Zabriskie, J.B.2
  • 144
    • 0031985944 scopus 로고    scopus 로고
    • Streptokinase as a mediator of acute post-streptococcal glomerulonephritis in an experimental mouse model
    • Nordstrand A, Norgren M, Ferretti JJ, Holm SE. Streptokinase as a mediator of acute post-streptococcal glomerulonephritis in an experimental mouse model. Infect Immun 1998; 66: 315-21.
    • (1998) Infect Immun , vol.66 , pp. 315-321
    • Nordstrand, A.1    Norgren, M.2    Ferretti, J.J.3    Holm, S.E.4
  • 145
    • 0027051734 scopus 로고
    • Failure to detect unique reactivity to streptococcal streptokinase in either the sera or renal biopsy specimens of patients with acute poststreptococcal glomerulonephritis
    • Mezzano S, Burgos E, Mahabir R, Kemeny E, Zabriskie JB. Failure to detect unique reactivity to streptococcal streptokinase in either the sera or renal biopsy specimens of patients with acute poststreptococcal glomerulonephritis. Clin Nephrof 1992; 38: 305-10.
    • (1992) Clin Nephrof , vol.38 , pp. 305-310
    • Mezzano, S.1    Burgos, E.2    Mahabir, R.3    Kemeny, E.4    Zabriskie, J.B.5
  • 148
    • 0003745052 scopus 로고    scopus 로고
    • Vaccine approaches to protect against group A streptococcal pharyngitis
    • Fischetti VA, et al, eds. Washington, DC: American Society for Microbiology
    • Fischetti VA. Vaccine approaches to protect against group A streptococcal pharyngitis. In: Fischetti VA, et al, eds. Gram-positive pathogens. Washington, DC: American Society for Microbiology, 2000: 96-104.
    • (2000) Gram-Positive Pathogens , pp. 96-104
    • Fischetti, V.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.