메뉴 건너뛰기




Volumn 187, Issue 3, 2003, Pages 398-407

Selective modulation of superantigen-induced responses by streptococcal cysteine protease

Author keywords

[No Author keywords available]

Indexed keywords

AGMATINE; CYSTEINE PROTEINASE; EXOTOXIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; STREPTOCOCCAL PYROGENIC EXOTOXIN; SUPERANTIGEN; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 0037312503     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1086/368022     Document Type: Article
Times cited : (46)

References (30)
  • 1
    • 0002640017 scopus 로고    scopus 로고
    • The re-emergence of severe group A streptococcal disease: An evolutionary perspective
    • Low DE, Schwartz B, McGeer A. The re-emergence of severe group A streptococcal disease: an evolutionary perspective. Emerg Pathog 1997; 1:93-123.
    • (1997) Emerg Pathog , vol.1 , pp. 93-123
    • Low, D.E.1    Schwartz, B.2    McGeer, A.3
  • 2
    • 0029114579 scopus 로고
    • Bacterial pyrogenic exotoxins as superantigens
    • Kotb M. Bacterial pyrogenic exotoxins as superantigens. Clin Microbiol Rev 1995; 8:411-26.
    • (1995) Clin Microbiol Rev , vol.8 , pp. 411-426
    • Kotb, M.1
  • 3
    • 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
  • 4
    • 0033808289 scopus 로고    scopus 로고
    • Host-microbe interactions in the pathogenesis of invasive group A streptococcal infections
    • Norrby-Teglund A, Kotb M. Host-microbe interactions in the pathogenesis of invasive group A streptococcal infections. J Med Microbiol 2000; 49:849-52.
    • (2000) J Med Microbiol , vol.49 , pp. 849-852
    • Norrby-Teglund, A.1    Kotb, M.2
  • 5
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge A, Bjorck L. Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J Biol Chem 1995; 270:9862-7.
    • (1995) J Biol Chem , vol.270 , pp. 9862-9867
    • Berge, A.1    Bjorck, L.2
  • 6
    • 0030037566 scopus 로고    scopus 로고
    • Severe invasive group A streptococcal disease: Clinical description and mechanisms of pathogenesis
    • Schlievert PM, Assimacopoulos AP, Cleary PP. Severe invasive group A streptococcal disease: clinical description and mechanisms of pathogenesis. J Lab Clin Med 1996; 127:13-22.
    • (1996) J Lab Clin Med , vol.127 , pp. 13-22
    • Schlievert, P.M.1    Assimacopoulos, A.P.2    Cleary, P.P.3
  • 7
    • 0034033679 scopus 로고    scopus 로고
    • Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases
    • Chatellier S, Ihendyane N, Kansal RG, et al. Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases. Infect Immun 2000; 68:3523-34.
    • (2000) Infect Immun , vol.68 , pp. 3523-3534
    • Chatellier, S.1    Ihendyane, N.2    Kansal, R.G.3
  • 8
    • 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: 6362-9.
    • (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
  • 9
    • 0034926023 scopus 로고    scopus 로고
    • Reciprocal, temporal expression of SpeA and SpeB by invasive M1T1 group a streptococcal isolates in vivo
    • Kazmi SU, Kansal R, Aziz RK, et al. Reciprocal, temporal expression of SpeA and SpeB by invasive M1T1 group a streptococcal isolates in vivo. Infect Immun 2001; 69:4988-95.
    • (2001) Infect Immun , vol.69 , pp. 4988-4995
    • Kazmi, S.U.1    Kansal, R.2    Aziz, R.K.3
  • 10
    • 10244261522 scopus 로고    scopus 로고
    • Activation of 66-kilodalton human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine protease
    • Burns EH Jr, Marciel AM, Musser JM. Activation of 66-kilodalton human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine protease. Infect Immun 1996; 64:4744-50.
    • (1996) Infect Immun , vol.64 , pp. 4744-4750
    • Burns E.H., Jr.1    Marciel, A.M.2    Musser, J.M.3
  • 11
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A virulence mechanism
    • Herwald H, Collin M, Muller-Esterl W, Bjorck L. Streptococcal cysteine proteinase releases kinins: a 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
  • 12
    • 0027290733 scopus 로고
    • Cleavage of interleukin 1β (IL-1β) precursor to produce active IL 1-β by a conserved extracellular cysteine protease from Streptococcus pyogenes
    • Kapur V, Majesky MW, Li L-L, Black RA, Musser JM. Cleavage of interleukin 1β (IL-1β) precursor to produce active IL 1-β 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
  • 13
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kaput V, Topouzis S, Majesky MW, et al. A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin. Microb Pathog 1993; 15:327-46.
    • (1993) Microb Pathog , vol.15 , pp. 327-346
    • Kaput, V.1    Topouzis, S.2    Majesky, M.W.3
  • 14
    • 0028032258 scopus 로고
    • Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface
    • Wolf BB, Gibson CA, Kapur V, Hussaini IM, Musser JM, Gonias SL. Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface. J Biol Chem 1994; 269:30682-7.
    • (1994) J Biol Chem , vol.269 , pp. 30682-30687
    • Wolf, B.B.1    Gibson, C.A.2    Kapur, V.3    Hussaini, I.M.4    Musser, J.M.5    Gonias, S.L.6
  • 15
    • 0034038360 scopus 로고    scopus 로고
    • Streptococcal erythrogenic toxin B brogates fibronectin-dependent internalization of Streptococcus pyogenes by cultured mammalian cells
    • Chaussee MS, Cole RL, van Putten JP. Streptococcal erythrogenic toxin B brogates fibronectin-dependent internalization of Streptococcus pyogenes by cultured mammalian cells. Infect Immun 2000; 68:3226-32.
    • (2000) Infect Immun , vol.68 , pp. 3226-3232
    • Chaussee, M.S.1    Cole, R.L.2    Van Putten, J.P.3
  • 16
    • 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, Boyle MD. A secreted streptococcal cysteine protease can cleave a surface-expressed M1 protein and alter the immunoglobulin binding properties. Res Microbiol 1998; 149:539-48.
    • (1998) Res Microbiol , vol.149 , pp. 539-548
    • Raeder, R.1    Woischnik, M.2    Podbielski, A.3    Boyle, M.D.4
  • 17
    • 0033978769 scopus 로고    scopus 로고
    • Absence of SpeB production in virulent large capsular forms of group A streptococcal strain 64
    • Raeder R, Harokopakis E, Hollingshead S, Boyle MD. Absence of SpeB production in virulent large capsular forms of group A streptococcal strain 64. Infect Immun 2000; 68:744-51.
    • (2000) Infect Immun , vol.68 , pp. 744-751
    • Raeder, R.1    Harokopakis, E.2    Hollingshead, S.3    Boyle, M.D.4
  • 18
    • 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
  • 19
    • 0033042528 scopus 로고    scopus 로고
    • Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice
    • Lukomski S, Montgomery CA, Rurangirwa J, et al. Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice. Infect Immun 1999; 67:1779-88.
    • (1999) Infect Immun , vol.67 , pp. 1779-1788
    • Lukomski, S.1    Montgomery, C.A.2    Rurangirwa, J.3
  • 20
    • 0030960001 scopus 로고    scopus 로고
    • Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serottype M3 and M49 strains
    • Lukomski S, Sreevatsan S, Amberg C, et al. Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serottype M3 and M49 strains. J Clin Invest 1997;99:2574-80.
    • (1997) J Clin Invest , vol.99 , pp. 2574-2580
    • Lukomski, S.1    Sreevatsan, S.2    Amberg, C.3
  • 21
    • 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 Infect Immun
    • Lukomski S, Burns EH Jr, 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; 66:771-6.
    • (1998) , vol.66 , pp. 771-776
    • Lukomski, S.1    Burns E.H., Jr.2    Wyde, P.R.3
  • 22
    • 0034777396 scopus 로고    scopus 로고
    • Absence of a cysteine protease effect on bacterial virulence in two murine models of human invasive group A streptococcal infection
    • Ashbaugh CD, Wessels MR. Absence of a cysteine protease effect on bacterial virulence in two murine models of human invasive group A streptococcal infection. Infect Immun 2001; 69:6683-8.
    • (2001) Infect Immun , vol.69 , pp. 6683-6688
    • Ashbaugh, C.D.1    Wessels, M.R.2
  • 23
    • 0030868740 scopus 로고    scopus 로고
    • New genetic techniques for group B streptococci: High-efficiency transformation, maintenance of temperature-sensitive pWV01 plasmids, and mutagenesis with Tn917
    • Framson PE, Nittayajarn A, Merry J, Youngman P, Rubens CE. New genetic techniques for group B streptococci: high-efficiency transformation, maintenance of temperature-sensitive pWV01 plasmids, and mutagenesis with Tn917. Appl Environ Microbiol 1997; 63:3539-47.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3539-3547
    • Framson, P.E.1    Nittayajarn, A.2    Merry, J.3    Youngman, P.4    Rubens, C.E.5
  • 24
    • 0030584899 scopus 로고    scopus 로고
    • Plasma from patients with severe invasive group A streptococcal infections treated with normal polyspecific IgG inhibits streptococcal superantigen-induced T cell proliferation and cytokine production
    • Norrby-Teglund A, Kaul R, Low DE, et al. Plasma from patients with severe invasive group A streptococcal infections treated with normal polyspecific IgG inhibits streptococcal superantigen-induced T cell proliferation and cytokine production. J Immunol 1996; 156:3057-64.
    • (1996) J Immunol , vol.156 , pp. 3057-3064
    • Norrby-Teglund, A.1    Kaul, R.2    Low, D.E.3
  • 25
    • 0033521608 scopus 로고    scopus 로고
    • Identification and characterization of novel superantigens from Streptococcus pyogenes
    • Proft T, Moffatt SL, Berkahn CJ, Fraser JD. Identification and characterization of novel superantigens from Streptococcus pyogenes. J Exp Med 1999; 189:89-102.
    • (1999) J Exp Med , vol.189 , pp. 89-102
    • Proft, T.1    Moffatt, S.L.2    Berkahn, C.J.3    Fraser, J.D.4
  • 26
    • 0026658912 scopus 로고
    • Role of superantigens in the pathogenesis of infectious diseases and their sequelae
    • Kotb M. Role of superantigens in the pathogenesis of infectious diseases and their sequelae. Curr Opin Infect Dis 1992; 5:364-74.
    • (1992) Curr Opin Infect Dis , vol.5 , pp. 364-374
    • Kotb, M.1
  • 27
    • 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
  • 28
    • 0034658411 scopus 로고    scopus 로고
    • The streptococcal superantigen SMEZ exhibits wide allelic variation, mosaic structure, and significant antigenic variation
    • Proft T, Moffatt SL, Weller KD, Paterson A, Martin D, Fraser JD. The streptococcal superantigen SMEZ exhibits wide allelic variation, mosaic structure, and significant antigenic variation. J Exp Med 2000; 191: 1765-76.
    • (2000) J Exp Med , vol.191 , pp. 1765-1776
    • Proft, T.1    Moffatt, S.L.2    Weller, K.D.3    Paterson, A.4    Martin, D.5    Fraser, J.D.6
  • 29
    • 0037007214 scopus 로고    scopus 로고
    • IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
    • von Pawel-Rammingen U, Johansson BP, Bjorck L. IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. EMBO J 2002; 21:1607-15.
    • (2002) EMBO J , vol.21 , pp. 1607-1615
    • Von Pawel-Rammingen, U.1    Johansson, B.P.2    Bjorck, L.3
  • 30
    • 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; 169:2561-9.
    • (2002) J Immunol , vol.169 , pp. 2561-2569
    • Unnikrishnan, M.1    Altmann, D.M.2    Proft, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.