메뉴 건너뛰기




Volumn 20, Issue 10, 2006, Pages

Trigger for group A streptococcal M1T1 invasive disease

Author keywords

Plasminogen; SpeB; Streptococcus pyogenes

Indexed keywords

PLASMIN;

EID: 33845633871     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.06-5804fje     Document Type: Article
Times cited : (134)

References (37)
  • 1
    • 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
  • 2
    • 0026580187 scopus 로고
    • Invasive group A Streptococcus infections
    • Stevens, D. L. (1992) Invasive group A Streptococcus infections. Clin. Infect. Dis. 14, 2-11
    • (1992) Clin. Infect. Dis. , vol.14 , pp. 2-11
    • Stevens, D.L.1
  • 3
    • 0036605511 scopus 로고    scopus 로고
    • A comparison of group A streptococci from invasive and uncomplicated infections: Are virulent clones responsible for serious streptococcal infections?
    • Johnson, D. R., Wotton, J. T., Shet, A., and Kaplan, E. L. (2002) A comparison of group A streptococci from invasive and uncomplicated infections: Are virulent clones responsible for serious streptococcal infections? J. Infect. Dis. 185, 1586-1595
    • (2002) J. Infect. Dis. , vol.185 , pp. 1586-1595
    • Johnson, D.R.1    Wotton, J.T.2    Shet, A.3    Kaplan, E.L.4
  • 4
    • 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., McGeer, A., Low, D. E., Norrby-Teglund, A., and Kotb, M. (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
  • 5
    • 0029889570 scopus 로고    scopus 로고
    • Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1β convertase) alters proteolytic activity and ablates zymogen processing
    • Musser, J., Stockbauer, K., Kapur, V., and Rudgers, G. (1996) Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1β convertase) alters proteolytic activity and ablates zymogen processing. Infect. Immun. 64, 1913-1917
    • (1996) Infect. Immun. , vol.64 , pp. 1913-1917
    • Musser, J.1    Stockbauer, K.2    Kapur, V.3    Rudgers, G.4
  • 6
    • 22644440878 scopus 로고    scopus 로고
    • Virulence factors of the group A streptococci and genes that regulate their expression
    • Hynes, W. (2004) Virulence factors of the group A streptococci and genes that regulate their expression. Front. Biosci. 9, 3399-3433
    • (2004) Front. Biosci. , vol.9 , pp. 3399-3433
    • Hynes, W.1
  • 7
    • 11144237617 scopus 로고    scopus 로고
    • 2-Macroglobulin-proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37
    • 2-Macroglobulin-proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37. J. Biol. Chem. 279, 52820-52823
    • (2004) J. Biol. Chem. , vol.279 , pp. 52820-52823
    • Nyberg, P.1    Rasmussen, M.2    Björck, L.3
  • 8
    • 0033744193 scopus 로고    scopus 로고
    • Role for a secreted cysteine proteinase in the establishment of host tissue tropism by group A streptococci
    • Svensson, M. D., Scaramuzzino, D. A., Sjöbring, U., Olsen, A., Frank, C., and Bessen, D. E. (2000) Role for a secreted cysteine proteinase in the establishment of host tissue tropism by group A streptococci. Mol. Microbiol. 38, 242-253
    • (2000) Mol. Microbiol. , vol.38 , pp. 242-253
    • Svensson, M.D.1    Scaramuzzino, D.A.2    Sjöbring, U.3    Olsen, A.4    Frank, C.5    Bessen, D.E.6
  • 9
    • 0033779403 scopus 로고    scopus 로고
    • A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance
    • Ringdahl, U., Svensson, H. G., Kotarsky, H., Gustafsson, M., Weineisen, M., and Sjöbring, U. (2000) A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance. Mol. Microbiol. 37, 1318-1326
    • (2000) Mol. Microbiol. , vol.37 , pp. 1318-1326
    • Ringdahl, U.1    Svensson, H.G.2    Kotarsky, H.3    Gustafsson, M.4    Weineisen, M.5    Sjöbring, U.6
  • 10
    • 0032434852 scopus 로고    scopus 로고
    • A secreted streptococcal cysteine protease can cleave a surface-expressed M1 protein and alter the immunoglobulin binding properties
    • Raeder, R., Woischnik, M., Podbielski, A., and Boyle, M. D. (1998) A secreted 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.4
  • 11
    • 0037312503 scopus 로고    scopus 로고
    • Selective modulation of superantigen-induced responses by streptococcal cysteine protease
    • Kansal, R. G., Nizet, V., Jeng, A., Chuang, W. J., and Kotb, M. (2003) Selective modulation of superantigen-induced responses by streptococcal cysteine protease. J. Infect. Dis. 187, 398-407
    • (2003) J. Infect. Dis. , vol.187 , pp. 398-407
    • Kansal, R.G.1    Nizet, V.2    Jeng, A.3    Chuang, W.J.4    Kotb, M.5
  • 12
    • 0347595329 scopus 로고    scopus 로고
    • Invasive M1T1 group A Streptococcus undergoes a phase-shift in vivo to prevent proteolytic degradation of multiple virulence factors by SpeB
    • Aziz, R. K., Pabst, M. J., Jeng, A., Kansal, R., Low, D. E., Nizet, V., and Kotb, M. (2004) Invasive M1T1 group A Streptococcus undergoes a phase-shift in vivo to prevent proteolytic degradation of multiple virulence factors by SpeB. Mol. Microbiol. 51, 123-134
    • (2004) Mol. Microbiol. , vol.51 , pp. 123-134
    • Aziz, R.K.1    Pabst, M.J.2    Jeng, A.3    Kansal, R.4    Low, D.E.5    Nizet, V.6    Kotb, M.7
  • 13
    • 1242318719 scopus 로고    scopus 로고
    • Mouse skin passage of Streptococcus pyogenes results in increased streptokinase expression and activity
    • Rezcallah, M. S., Boyle, M. D., and Sledjeski, D. D. (2004) Mouse skin passage of Streptococcus pyogenes results in increased streptokinase expression and activity. Microbiology 150, 365-371
    • (2004) Microbiology , vol.150 , pp. 365-371
    • Rezcallah, M.S.1    Boyle, M.D.2    Sledjeski, D.D.3
  • 16
    • 21244444520 scopus 로고    scopus 로고
    • Is plasminogen deployed as a Streptococcus pyogenes virulence factor?
    • Walker, M. J., McArthur, J. D., McKay, F., and Ranson, M. (2005) Is plasminogen deployed as a Streptococcus pyogenes virulence factor? Trends. Microbiol. 13, 308-313
    • (2005) Trends Microbiol. , vol.13 , pp. 308-313
    • Walker, M.J.1    McArthur, J.D.2    McKay, F.3    Ranson, M.4
  • 18
    • 0029957927 scopus 로고    scopus 로고
    • Hyaluronic acid capsule and the role of streptococcal entry into keratinocytes in invasive skin infection
    • Schrager, H. M., Rheinwald, J. G., and Wessels, M. R. (1996) Hyaluronic acid capsule and the role of streptococcal entry into keratinocytes in invasive skin infection. J. Clin. Invest. 98, 1954-1958
    • (1996) J. Clin. Invest. , vol.98 , pp. 1954-1958
    • Schrager, H.M.1    Rheinwald, J.G.2    Wessels, M.R.3
  • 19
    • 0035151019 scopus 로고    scopus 로고
    • The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strep-adhesin, laminin-binding and cysteine protease activity
    • Hytönen, J., Haataja, S., Gerlach, D., Podbielski, A., and Finne, J. (2001) The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strep-adhesin, laminin-binding and cysteine protease activity. Mol. Microbiol. 39, 512-519
    • (2001) Mol. Microbiol. , vol.39 , pp. 512-519
    • Hytönen, J.1    Haataja, S.2    Gerlach, D.3    Podbielski, A.4    Finne, J.5
  • 20
    • 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, C. D., Warren, H. B., Carey, V. J., and Wessels, M. R. (1998) 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. 102, 550-560
    • (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
  • 21
    • 0027957897 scopus 로고
    • Analysis of plasmin(ogen) acquisition by clinical isolates of group A streptococci incubated in human plasma
    • Wang, H., Lottenberg, R., and Boyle, M. D. (1994) Analysis of plasmin(ogen) acquisition by clinical isolates of group A streptococci incubated in human plasma. J. Infect. Dis. 169, 143-149
    • (1994) J. Infect. Dis. , vol.169 , pp. 143-149
    • Wang, H.1    Lottenberg, R.2    Boyle, M.D.3
  • 22
    • 17644397901 scopus 로고    scopus 로고
    • Surface analyses and immune reactivities of major cell wall-associated proteins of group A Streptococcus
    • Cole, J. N., Ramirez, R. D., Currie, B. J., Cordwell, S. J., Djordjevic, S. P., and Walker, M. J. (2005) Surface analyses and immune reactivities of major cell wall-associated proteins of group A Streptococcus. Infect. Immun. 73, 3137-3146
    • (2005) Infect. Immun. , vol.73 , pp. 3137-3146
    • Cole, J.N.1    Ramirez, R.D.2    Currie, B.J.3    Cordwell, S.J.4    Djordjevic, S.P.5    Walker, M.J.6
  • 23
    • 0036150446 scopus 로고    scopus 로고
    • Immunological response mounted by Aboriginal Australians living in the Northern Territory of Australia against Streptococcus pyogenes serum opacity factor
    • Gillen, C. M., Towers, R. J., McMillan, D. J., Delvecchio, A., Sriprakash, K. S., Currie, B., Kreikemeyer, B., Chhatwal, G. S., and Walker, M. J. (2002) Immunological response mounted by Aboriginal Australians living in the Northern Territory of Australia against Streptococcus pyogenes serum opacity factor. Microbiology 148, 169-178
    • (2002) Microbiology , vol.148 , pp. 169-178
    • Gillen, C.M.1    Towers, R.J.2    McMillan, D.J.3    Delvecchio, A.4    Sriprakash, K.S.5    Currie, B.6    Kreikemeyer, B.7    Chhatwal, G.S.8    Walker, M.J.9
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0019551730 scopus 로고
    • Western blotting: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. (1981) Western blotting: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 28
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch, J., and Caparon, M. (2004) A microdomain for protein secretion in Gram-positive bacteria. Science 304, 1513-1515
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 29
    • 0032486286 scopus 로고    scopus 로고
    • Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., and Fischetti, V. A. (1998) α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273, 14503-14515
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 30
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3- phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., and Fischetti, V. (1992) A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 176, 415- 426
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.2
  • 31
    • 0028797210 scopus 로고
    • A role for fibrinogen in the streptokinase-dependent acquisition of plasmin(ogen) by group A streptococci
    • Wang, H., Lottenberg, R., and Boyle, M. D. (1995) A role for fibrinogen in the streptokinase-dependent acquisition of plasmin(ogen) by group A streptococci. J. Infect. Dis. 171, 85-92
    • (1995) J. Infect. Dis. , vol.171 , pp. 85-92
    • Wang, H.1    Lottenberg, R.2    Boyle, M.D.3
  • 32
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb, Z. (1997) ECM and cell surface proteolysis: regulating cellular ecology. Cell 91, 439-442
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 33
    • 0027451350 scopus 로고
    • PAM, a novel plasminogen-binding protein from Streptococcus pyogenes
    • Berge, A., and Sjöbring, U. (1993) PAM, a novel plasminogen-binding protein from Streptococcus pyogenes. J. Biol. Chem. 268, 25417-25424
    • (1993) J. Biol. Chem. , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjöbring, U.2
  • 34
    • 0026673916 scopus 로고
    • Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor
    • Lottenberg, R., Broder, C. C., Boyle, M. D., Kain, S. J., Schroeder, B. L., and Curtiss, R., 3rd (1992) Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor. J. Bacteriol. 174, 5204-5210
    • (1992) J. Bacteriol. , vol.174 , pp. 5204-5210
    • Lottenberg, R.1    Broder, C.C.2    Boyle, M.D.3    Kain, S.J.4    Schroeder, B.L.5    Curtiss III, R.6
  • 35
    • 0029039458 scopus 로고
    • Analysis of the interaction of group A streptococci with fibrinogen, streptokinase and plasminogen
    • Wang, H., Lottenberg, R., and Boyle, M. D. (1995) Analysis of the interaction of group A streptococci with fibrinogen, streptokinase and plasminogen. Microb. Pathog. 18, 153-166
    • (1995) Microb. Pathog. , vol.18 , pp. 153-166
    • Wang, H.1    Lottenberg, R.2    Boyle, M.D.3
  • 36
    • 0031042682 scopus 로고    scopus 로고
    • Plasminogen activation by invasive human pathogens
    • Boyle, M. D., and Lottenberg, R. (1997) Plasminogen activation by invasive human pathogens. Thromb. Haemost. 77, 1-10
    • (1997) Thromb. Haemost. , vol.77 , pp. 1-10
    • Boyle, M.D.1    Lottenberg, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.