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Volumn 73, Issue 2, 2005, Pages 859-864

The M protein is dispensable for maturation of streptococcal cysteine protease SpeB

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL M PROTEIN; BACTERIAL M1 PROTEIN; BACTERIAL PROTEIN; CYSTEINE PROTEINASE; EXOTOXIN; STREPTOCOCCAL PYROGENIC EXOTOXIN B; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 12844282320     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.2.859-864.2005     Document Type: Article
Times cited : (11)

References (52)
  • 1
    • 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, C. D., T. J. Moser, M. H. Shearer, G. L. White, R. C. Kennedy, and M. R. Wessels. 2000. Bacterial determinants of persistent throat colonization and the associated immune response in a primate model of human group A streptococcal pharyngeal infection. Cell Microbiol. 2:283-292.
    • (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
  • 2
    • 0032774759 scopus 로고    scopus 로고
    • Stress-induced membrane association of the Streptococcus mutans GTP-binding protein, an essential G protein, and investigation of its physiological role by utilizing an antisense RNA strategy
    • Baev, D., R. England, and H. K. Kuramitsu. 1999. Stress-induced membrane association of the Streptococcus mutans GTP-binding protein, an essential G protein, and investigation of its physiological role by utilizing an antisense RNA strategy. Infect. Immun. 67:4510-4516.
    • (1999) Infect. Immun. , vol.67 , pp. 4510-4516
    • Baev, D.1    England, R.2    Kuramitsu, H.K.3
  • 3
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge, A., and L. Björck. 1995. Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J. Biol. Chem. 270:9862-9867.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9862-9867
    • Berge, A.1    Björck, L.2
  • 4
    • 0027151798 scopus 로고
    • High-efficiency gene inactivation and replacement system for gram-positive bacteria
    • Biswas, I., A. Gruss, S. D. Ehrlich, and E. Maguin. 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
    • 0023903986 scopus 로고
    • Cloning of the gene speB for streptococcal pyrogenic exotoxin type B in Escherichia coli
    • Bohach, G. A., A. R. Hauser, and P. M. Schlievert. 1988. Cloning of the gene speB for streptococcal pyrogenic exotoxin type B in Escherichia coli. Infect. Immun. 56:1665-1667.
    • (1988) Infect. Immun. , vol.56 , pp. 1665-1667
    • Bohach, G.A.1    Hauser, A.R.2    Schlievert, P.M.3
  • 6
    • 0025774825 scopus 로고
    • Role of M protein in adherence of group A streptococci
    • Caparon, M. G., D. S. Stephens, A. Olsen, and J. R. Scott. 1991. Role of M protein in adherence of group A streptococci. Infect. Immun. 59:1811-1817.
    • (1991) Infect. Immun. , vol.59 , pp. 1811-1817
    • Caparon, M.G.1    Stephens, D.S.2    Olsen, A.3    Scott, J.R.4
  • 7
    • 0030948560 scopus 로고    scopus 로고
    • Temporal production of streptococcal erythrgenic toxin B (streptococcal cysteine protease) in response to nutrient depletion
    • Chaussee, M. S., E. R. Phillips, and J. J. Ferretti. 1997. Temporal production of streptococcal erythrgenic toxin B (streptococcal cysteine protease) in response to nutrient depletion. Infect. Immun. 65:1956-1959.
    • (1997) Infect. Immun. , vol.65 , pp. 1956-1959
    • Chaussee, M.S.1    Phillips, E.R.2    Ferretti, J.J.3
  • 9
    • 0033923852 scopus 로고    scopus 로고
    • Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein
    • Collin, M., and A. Olsen. 2000. Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein. Mol. Microbiol. 36:1306-1318.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1306-1318
    • Collin, M.1    Olsen, A.2
  • 10
    • 0034773523 scopus 로고    scopus 로고
    • Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins
    • Collin, M., and A. Olsen. 2001. Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins. Infect. Immun. 69:7187-7189.
    • (2001) Infect. Immun. , vol.69 , pp. 7187-7189
    • Collin, M.1    Olsen, A.2
  • 11
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • Collin, M., and A. Olsen. 2001. EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J. 20:3046-3055.
    • (2001) EMBO J. , vol.20 , pp. 3046-3055
    • Collin, M.1    Olsen, A.2
  • 12
    • 0031684402 scopus 로고    scopus 로고
    • Immunohistochemical and serological evidence for the role of streptococcal proteinase in acute-poststreptococcal glomerulonephritis
    • Cu, G. A., S. Mezzano, J. D. Bannan, and J. B. Zabriskie. 1998. Immunohistochemical and serological evidence for the role of streptococcal proteinase in acute-poststreptococcal glomerulonephritis. Kidney Int. 54:819-826.
    • (1998) Kidney Int. , vol.54 , pp. 819-826
    • Cu, G.A.1    Mezzano, S.2    Bannan, J.D.3    Zabriskie, J.B.4
  • 13
    • 0035188080 scopus 로고    scopus 로고
    • Genetic dissection of the Streptococcus pyogenes M1 protein: Regions involved in fibronectin binding and intracelluar invasion
    • Cue, D., H. Lam, and P. P. Cleary. 2001. Genetic dissection of the Streptococcus pyogenes M1 protein: regions involved in fibronectin binding and intracelluar invasion. Microb. Pathog. 31:231-242.
    • (2001) Microb. Pathog. , vol.31 , pp. 231-242
    • Cue, D.1    Lam, H.2    Cleary, P.P.3
  • 14
    • 0030908268 scopus 로고    scopus 로고
    • High-frequency invasion of epithelial cells by Streptococcus pyogenes can be activated by fibrinogen and peptides containing the sequence RGD
    • Cue, D. R., and P. P. Cleary. 1997. High-frequency invasion of epithelial cells by Streptococcus pyogenes can be activated by fibrinogen and peptides containing the sequence RGD. Infect. Immun. 65:2759-2764.
    • (1997) Infect. Immun. , vol.65 , pp. 2759-2764
    • Cue, D.R.1    Cleary, P.P.2
  • 15
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M. W. 2000. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13:470-511.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 16
    • 0034971985 scopus 로고    scopus 로고
    • Design of a protein-targeting system for lactic acid bacteria
    • Dieye, Y., S. Usai, F. Clier, A. Gruss, and J. C. Piard. 2001. Design of a protein-targeting system for lactic acid bacteria. J. Bacteriol. 183:4157-4166.
    • (2001) J. Bacteriol. , vol.183 , pp. 4157-4166
    • Dieye, Y.1    Usai, S.2    Clier, F.3    Gruss, A.4    Piard, J.C.5
  • 17
    • 0032904116 scopus 로고    scopus 로고
    • High-frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements
    • Dombek, P. E., D. Cue, J. Sedgewick, H. Lam, S. Ruschkowski, B. B. Finlay, and P. P. Cleary. 1999. High-frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements. Mol. Microbiol. 31:859-870.
    • (1999) Mol. Microbiol. , vol.31 , pp. 859-870
    • Dombek, P.E.1    Cue, D.2    Sedgewick, J.3    Lam, H.4    Ruschkowski, S.5    Finlay, B.B.6    Cleary, P.P.7
  • 19
    • 0001322321 scopus 로고
    • A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen
    • Elliott, S. D. 1945. A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen. J. Exp. Med. 81:573-592.
    • (1945) J. Exp. Med. , vol.81 , pp. 573-592
    • Elliott, S.D.1
  • 20
    • 0000647519 scopus 로고
    • An inactive precursor of streptococcal proteinase
    • Elliott, S. D., and V. P. Dole. 1947. An inactive precursor of streptococcal proteinase. J. Exp. Med. 85:305-320.
    • (1947) J. Exp. Med. , vol.85 , pp. 305-320
    • Elliott, S.D.1    Dole, V.P.2
  • 22
    • 0033053646 scopus 로고    scopus 로고
    • A response regulator that represses transcription of several virulence operons in the group A Streptococcus
    • Federle, M. J., K. S. McIver, and J. R. Scott. 1999. A response regulator that represses transcription of several virulence operons in the group A Streptococcus. J. Bacteriol. 181:3649-3657.
    • (1999) J. Bacteriol. , vol.181 , pp. 3649-3657
    • Federle, M.J.1    McIver, K.S.2    Scott, J.R.3
  • 23
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti, V. A. 1989. Streptococcal M protein: molecular design and biological behavior. Clin. Microbiol. Rev. 2:285-314.
    • (1989) Clin. Microbiol. Rev. , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 24
    • 0031930829 scopus 로고    scopus 로고
    • Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes
    • Gubba, S., D. E. Low, and J. M. Musser. 1998. Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes. Infect. Immun. 66:765-770.
    • (1998) Infect. Immun. , vol.66 , pp. 765-770
    • Gubba, S.1    Low, D.E.2    Musser, J.M.3
  • 25
    • 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., V. J. DiRita, N. L. Barg, and N. C. Engleberg. 1999. 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. 67:5298-5305.
    • (1999) Infect. Immun. , vol.67 , pp. 5298-5305
    • Heath, A.1    DiRita, V.J.2    Barg, N.L.3    Engleberg, N.C.4
  • 26
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism
    • Herwald, H., M. Collin, W. Müller-Esterl, and L. Björck. 1996. Streptococcal cysteine proteinase releases kinins: a novel virulence mechanism. J. Exp. Med. 184:665-673.
    • (1996) J. Exp. Med. , vol.184 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Müller-Esterl, W.3    Björck, L.4
  • 27
    • 0026771289 scopus 로고
    • Aspects of pathogenesis of serious group A streptococcal infections in Sweden, 1988-1989
    • Holm, S. E., A. Norrby, A. M. Bergholm, and M. Norgren. 1992. Aspects of pathogenesis of serious group A streptococcal infections in Sweden, 1988-1989. J. Infect. Dis. 166:31-37.
    • (1992) J. Infect. Dis.. , vol.166 , pp. 31-37
    • Holm, S.E.1    Norrby, A.2    Bergholm, A.M.3    Norgren, M.4
  • 28
    • 0343017792 scopus 로고
    • Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H
    • Horstmann, R. D., H. J. Sievertsen, J. Knobloch, and V. A. Fischetti. 1988. Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc. Natl. Acad. Sci. USA 85:1657-1661.
    • (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
  • 29
    • 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., N. Schnitzler, E. DeMaster, and P. Cleary. 1998. Impact of M49, Mrp, Enn, and C5a peptidase proteins on colonization of the mouse oral mucosa by Streptococcus pyogenes. Infect. Immun. 66:5399-5405.
    • (1998) Infect. Immun. , vol.66 , pp. 5399-5405
    • Ji, Y.1    Schnitzler, N.2    DeMaster, E.3    Cleary, P.4
  • 30
    • 0034058370 scopus 로고    scopus 로고
    • Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine protease
    • Kagawa, T. F., J. C. Cooney, H. M. Baker, S. McSweeney, M. Liu, S. Gubba, J. M. Musser, and E. N. Baker. 2000. Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: an integrin-binding cysteine protease. Proc. Natl. Acad. Sci. USA 97:2235-2240.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2235-2240
    • Kagawa, T.F.1    Cooney, J.C.2    Baker, H.M.3    McSweeney, S.4    Liu, M.5    Gubba, S.6    Musser, J.M.7    Baker, E.N.8
  • 31
    • 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, R. G., A. McGeer, D. E. Low, A. Norrby-Teglund, and M. Kotb. 2000. 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. 68:6362-6369.
    • (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
  • 32
    • 0025728148 scopus 로고
    • The resurgence of group A streptococcal infections and their sequelae
    • Kaplan, E. L. 1991. The resurgence of group A streptococcal infections and their sequelae. Eur. J. Clin. Microbiol. Infect. Dis. 10:55-57.
    • (1991) Eur. J. Clin. Microbiol. Infect. Dis. , vol.10 , pp. 55-57
    • Kaplan, E.L.1
  • 33
    • 0027290733 scopus 로고
    • Cleavage of interleukin 1β (IL-1β) precursor to produce active Il-1β by a conserved extracellular cysteine protease from Streptococcus pyogenes
    • Kapur, V., M. W. Majesky, L. L. Li, R. A. Black, and J. M. Musser. 1993. Cleavage of interleukin 1β (IL-1β) precursor to produce active Il-1β by a conserved extracellular cysteine protease from Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA 90:7676-7680.
    • (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
  • 34
    • 0001197006 scopus 로고
    • Current knowledge of the type specific M antigens of group A streptococci
    • Lancefield, R. C. 1962. Current knowledge of the type specific M antigens of group A streptococci. J. Immunol. 89:307-313.
    • (1962) J. Immunol. , vol.89 , pp. 307-313
    • Lancefield, R.C.1
  • 35
    • 0032822538 scopus 로고    scopus 로고
    • Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins
    • Li, Z., D. D. Sledjeski, B. Kreikemeyer, A. Podbielski, and M. D. P. Boyle. 1999. Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins. J. Bacteriol. 181:6019-6027.
    • (1999) J. Bacteriol. , vol.181 , pp. 6019-6027
    • Li, Z.1    Sledjeski, D.D.2    Kreikemeyer, B.3    Podbielski, A.4    Boyle, M.D.P.5
  • 36
    • 0030960001 scopus 로고    scopus 로고
    • Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains
    • Lukomski, S., S. Sreevatsan, C. Amberg, W. Reichardt, M. Woischnik, A. Podbielski, and J. M. Musser. 1997. Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains. J. Clin. Investig. 99:2574-2580.
    • (1997) J. Clin. Investig. , vol.99 , pp. 2574-2580
    • Lukomski, S.1    Sreevatsan, S.2    Amberg, C.3    Reichardt, W.4    Woischnik, M.5    Podbielski, A.6    Musser, J.M.7
  • 37
    • 0038623056 scopus 로고    scopus 로고
    • Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease
    • Lyon, W. R., and M. G. Caparon. 2003. Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease. J. Bacteriol. 185:3661-3667.
    • (2003) J. Bacteriol. , vol.185 , pp. 3661-3667
    • Lyon, W.R.1    Caparon, M.G.2
  • 38
    • 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, W. R., C. M. Gibson, and M. G. Caparon. 1998. 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. 17:6263-6275.
    • (1998) EMBO J. , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 39
    • 0036203828 scopus 로고    scopus 로고
    • Prospective identification and treatment of children with pediatric autoimmune neuropsychiatric disorder associated with group A straptococcal infection (PANDAS)
    • Murphy, M. L., and M. E. Pichichero. 2002. Prospective identification and treatment of children with pediatric autoimmune neuropsychiatric disorder associated with group A straptococcal infection (PANDAS). Arch. Pediatr. Adolesc. Med. 156:356-361.
    • (2002) Arch. Pediatr. Adolesc. Med. , vol.156 , pp. 356-361
    • Murphy, M.L.1    Pichichero, M.E.2
  • 40
    • 0041387460 scopus 로고    scopus 로고
    • Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes
    • Neely, M. N., W. R. Lyon, D. L. Runft, and M. Caparon. 2003. Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes. J. Bacteriol. 185:5166-5174.
    • (2003) J. Bacteriol. , vol.185 , pp. 5166-5174
    • Neely, M.N.1    Lyon, W.R.2    Runft, D.L.3    Caparon, M.4
  • 41
    • 0028674223 scopus 로고
    • Cysteine endopeptidases of parasitic protozoa
    • North, M. J. 1994. Cysteine endopeptidases of parasitic protozoa. Methods Enzymol. 244:523-539.
    • (1994) Methods Enzymol. , vol.244 , pp. 523-539
    • North, M.J.1
  • 42
    • 7244231206 scopus 로고    scopus 로고
    • Primary induction of CD4 T cell responses in nasal associated lymphoid tissue during group A streptococcal infection
    • Park, H.-S., M. Costalonga, R. L. Reinhardt, P. E. Dombek, M. K. Jenkins, and P. P. Cleary. 2004. Primary induction of CD4 T cell responses in nasal associated lymphoid tissue during group A streptococcal infection. Eur. J. Immunol. 34:2843-2854.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2843-2854
    • Park, H.-S.1    Costalonga, M.2    Reinhardt, R.L.3    Dombek, P.E.4    Jenkins, M.K.5    Cleary, P.P.6
  • 43
    • 0031776883 scopus 로고    scopus 로고
    • The group A streptococcal dipeptide permease (Dpp) is involved in uptake of essential amino acids and affects expression of cysteine protease
    • Podbielski, A., and B. A. B. Leonard. 1998. The group A streptococcal dipeptide permease (Dpp) is involved in uptake of essential amino acids and affects expression of cysteine protease. Mol. Microbiol. 28:1323-1334.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1323-1334
    • Podbielski, A.1    Leonard, B.A.B.2
  • 44
    • 0029798285 scopus 로고    scopus 로고
    • Molecular characterization of group A streptococcal (GAS) oligopeptide permease (Opp) and its effect on cysteine protease production
    • Podbielski, A., B. Pohl, M. Woischnik, C. Körner, K. H. Schmidt, E. Rozdzinski, and B. A. B. Leonard. 1996. Molecular characterization of group A streptococcal (GAS) oligopeptide permease (Opp) and its effect on cysteine protease production. Mol. Microbiol. 21:1087-1099.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1087-1099
    • Podbielski, A.1    Pohl, B.2    Woischnik, M.3    Körner, C.4    Schmidt, K.H.5    Rozdzinski, E.6    Leonard, B.A.B.7
  • 45
    • 0032746542 scopus 로고    scopus 로고
    • Cystein protease SpeB expression in group A streptococci is influenced by the nutritional environment but SpeB does not contribute to obtaining essential nutrients
    • Podbielski, A., M. Woischnik, B. Kreikemeyer, K. Bettenbrock, and L. Buttaro. 1999. Cystein protease SpeB expression in group A streptococci is influenced by the nutritional environment but SpeB does not contribute to obtaining essential nutrients. Med. Microbiol. Immunol. 188:99-109.
    • (1999) Med. Microbiol. Immunol. , vol.188 , pp. 99-109
    • Podbielski, A.1    Woischnik, M.2    Kreikemeyer, B.3    Bettenbrock, K.4    Buttaro, L.5
  • 46
    • 0030476579 scopus 로고    scopus 로고
    • What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors
    • Podbielski, A., M. Woischnik, B. Pohl, and K. H. Schmidt. 1996. What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors. Med. Microbiol. Immunol. 185:171-181.
    • (1996) Med. Microbiol. Immunol. , vol.185 , pp. 171-181
    • Podbielski, A.1    Woischnik, M.2    Pohl, B.3    Schmidt, K.H.4
  • 47
    • 0032434852 scopus 로고    scopus 로고
    • An extracellular streptococcal cysteine protease can cleave a surface expressed M1 protein and alter the immunoglobulin-binding properties
    • Raeder, R., M. Woischnik, A. Podbielski, and M. D. P. Boyle. 1998. An extracellular streptococcal cysteine protease can cleave a surface expressed M1 protein and alter the immunoglobulin-binding properties. Res. Microbiol. 149:539-548.
    • (1998) Res. Microbiol. , vol.149 , pp. 539-548
    • Raeder, R.1    Woischnik, M.2    Podbielski, A.3    Boyle, M.D.P.4
  • 48
    • 0037138799 scopus 로고    scopus 로고
    • Strep A, neuropsychiatric disorders tie found
    • Stephenson, J. 2002. Strep A, neuropsychiatric disorders tie found. JAMA 287:828.
    • (2002) JAMA , vol.287 , pp. 828
    • Stephenson, J.1
  • 49
    • 0029330062 scopus 로고
    • Streptococcal toxic-shock syndrome: Spectrum of disease, pathogenesis, and new concepts in treatment
    • Stevens, D. L. 1995. Streptococcal toxic-shock syndrome: spectrum of disease, pathogenesis, and new concepts in treatment. Emerg. Infect. Dis. 1:69-78.
    • (1995) Emerg. Infect. Dis. , vol.1 , pp. 69-78
    • Stevens, D.L.1
  • 50
    • 0027288421 scopus 로고
    • Association of phenotypic and genotypic characteristics of invasive Streptococcus pyogenes isolates with clinical components of streptococcal toxic shock syndrome
    • Talkington, D. F., B. Schwartz, C. M. Black, J. K. Todd, J. Elliott, R. F. Breiman, and R. R. Facklam. 1993. Association of phenotypic and genotypic characteristics of invasive Streptococcus pyogenes isolates with clinical components of streptococcal toxic shock syndrome. Infect. Immun. 61:3369-3374.
    • (1993) Infect. Immun. , vol.61 , pp. 3369-3374
    • Talkington, D.F.1    Schwartz, B.2    Black, C.M.3    Todd, J.K.4    Elliott, J.5    Breiman, R.F.6    Facklam, R.R.7
  • 51
    • 0034891203 scopus 로고    scopus 로고
    • Translocation of proteins across the cell envelope of gram-positive bacteria
    • van Wely, K. H. M., J. Swaving, R. Freundl, and A. J. M. Driessen. 2001. Translocation of proteins across the cell envelope of gram-positive bacteria. FEMS Microbiol. Rev. 25:437-454.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 437-454
    • Van Wely, K.H.M.1    Swaving, J.2    Freundl, R.3    Driessen, A.J.M.4
  • 52
    • 0026068847 scopus 로고
    • Frequency of the erythrogenic toxin B and C genes (speB and speC) among clinical isolates of group A streptococci
    • Yu, C., and J. J. Ferretti. 1991. Frequency of the erythrogenic toxin B and C genes (speB and speC) among clinical isolates of group A streptococci. Infect. Immun. 59:211-215.
    • (1991) Infect. Immun. , vol.59 , pp. 211-215
    • Yu, C.1    Ferretti, J.J.2


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