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Pyrogens streptococcal exotoxins

YuCE, Ferretti JJ Molecular epidemiologic analysis of the type A streptococcal exotoxin (erythrogenic toxin) gene (speA) in clinical Streptococcus pyogenes strains. Infect Immun 1989 57 3715-3719. Hauser A, Stevens D, Kaplan E, Schlievert P Molecular analysis of pyrogenic exotoxins from Streptococcus pyogenes isolates associated with toxic shock-like syndrome. J Clin Microbiol 1991 29 1562-1567. [Pg.21]

Brunson, K.W., Watson, D.W. Limulus amoebocyte lysate reaction with Streptococcal pyrogenic exotoxin. Infect Immun 14 (1976) 1256-1258. [Pg.203]

E, toxic shock syndrome toxin (TSST-1), the streptococcal pyrogenic exotoxins (SPE) A, B, Cs, G, and H, the streptococcal mitogenic exotoxins, SMEZ and SMEZ-2 are the best structurally studied superantigens thus far (Tables 5 and 6). [Pg.5162]

Watson D Host-parasite factors in group A streptococcal infections. Pyrogenic and other effects of immunologic distinct exotoxins related to scarlet fever toxins. J Exp Med 1960 111 255—284. [Pg.19]

Kim Y, Watson D A purified group A streptococcal pyrogenic exotoxin. Physiochemical and biological properties, including the enhancement of susceptibility to endotoxin lethal shock. J Exp Med 1970 131 611-622. [Pg.19]

Kreiswirth B, Handley J, Schlievert P, Novick R Cloning and expression of streptococcal pyrogenic exotoxin A and staphylococcal toxic shock syndrome toxin-1 in Bacillus subtilis. Mol Gen Genet 1987 208 84-87. [Pg.19]

Imanishi K, Igarashi H, UchiyamaT Activation of murine T cells by streptococcal pyrogenic exotoxin type A. Requirement for MHC class II molecules on accessory cells and identification ofV beta elements in T cell receptor of toxin-reactive T cells. J Immunol 1990 145 3170-3176. [Pg.19]

Bohach G, Hauser A, Schlievert P Cloning of the gene, speB, for streptococcal pyrogenic exotoxin type B in Escherichia coli. Infect Immun 1988 56 1665-1667. [Pg.19]

Leonard B, Lee P, Jenkins M, Schlievert PM Cell and receptor requirements for streptococcal pyrogenic exotoxin T cell mitogenicity. Infect Immun 1991 59 1210-1214. [Pg.19]

ProftT, Arcus Y Handley Y Baker E, Fraser J Immunological and biochemical characterization of streptococcal pyrogenic exotoxins I and J (SPE-I and SPE-J) from Streptococcus pyogenes. J Immun 2001 166 6711-6719. [Pg.20]

McCormick J, Pragman A, Stolpa J, Leung D, Schlievert P Functional characterization of streptococcal pyrogenic exotoxin J, a novel superantigen. Infect Immun 2001 69 1381-1388. [Pg.20]

Papageorgiou AC, Collins CM, Gutman DM, Kline JB, O Brian SM, Tranter HS, Acharya KR Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeA) by MHC class II molecules and T cell receptors. EMBO J 1999 18 9-21. [Pg.21]

Baker H, Proft T, Webb P, Arcus V, Fraser J, Baker E Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin 1 can use a common binding surface for T cell receptor binding and dimerization. 1 Biol Chem 2004 279 38571-38576. [Pg.21]

Li PL, Tiedemann RE, Moffat SL, Fraser JD The superantigen streptococcal pyrogenic exotoxin C (SPE-C) exhibits a novel mode of action. J Exp Med 1997 186 375-383. [Pg.21]

HsuehP, Wu J, TsaiP, Liu J, ChuangY, Luh K Invasive group A streptococcal disease in Taiwan is not associated with the presence of streptococcal pyrogenic exotoxin genes. Clin Infect Dis 1998 26 584-589. [Pg.22]

Sriskandan S, Moyes D, Buttery L, Krausz T, Evans T, Polak J, Cohen J Streptococcal pyrogenic exotoxin A release, distribution, and role in a murine model of fasciitis and multiorgan failure due to Streptococcus pyogenes. J Infect Dis 1996 173 1399-1407. [Pg.22]

Welcher B, Carra J, DaSilva L, Hanson J, David C, Aman M, Bavari S Lethal shock induced by streptococcal pyrogenic exotoxin A in mice transgenic for human leukocyte antigen-DQ8 and human CD4 receptors implications for development of vaccines and therapeutics. J Infect Dis 2002 186 501-510. [Pg.22]

Eriksson BKG, Andersson J, Holm SE, Norgren M Invasive group A streptococcal infections T1M1 isolates expressing pyrogenic exotoxins A and B in combination with selective lack of toxin-neutralizing antibodies are associated with increased risk of streptococcal toxic shock syndrome. J Infect Dis 1999 1X0 410 -IIS. [Pg.22]

McCormick JK, Tripp TJ, Olmsted SB, Matsuka YY Gahr PJ, Ohlendorf DH, Schlievert PM Development of streptococcal pyrogenic exotoxin C vaccine toxoids that are protective in the rabbit model of toxic shock syndrome. J Immunol 2000 165 2306-2312. [Pg.177]

Tripp TJ, McCormick JK, Webb JM, Schlievert PM The zinc-dependent major histocompatibility complex class II binding site of streptococcal pyrogenic exotoxin C is critical for maximal superantigen function and toxic activity. Infect Immun 2003 71 1548-1550. [Pg.177]

Brunson K.W. and Watson D.W. (1976) Limulus amebocyte lysate reaction with streptococcal pyrogenic exotoxin. Infect. Immun., 14, 1256-1258. [Pg.99]

Staphylococcal enterotoxin B (SEB) is one of seven enterotoxins produced by strains of Staphylococcus aureus. SEB, the best understood of the staphylococcal enterotoxins, can be regarded as the type enterotoxin. Staphylococcal enterotoxins, toxic shock syndrome toxin-1 (TSST-1), and certain other bacterial products (such as streptococcal pyrogenic exotoxins [SPE]) and viral products (which are not discussed in this chapter) are commonly referred to as superantigens because of their profound effects on the immune system. Minute concentrations of superantigens can activate the immune system receptors because they bind with strong avidity to T-cell antigen receptors and class II molecules of the major histocompatibility complex (MHC). [Pg.622]

Staphylococcal enterotoxin serotypes SEB, SEC1, SEC2, SEC3, and the streptococcal pyrogenic exotoxins A and C (SPE-A and SPE-C) form the second homology group. [Pg.622]

Betley MJ, Borst DW, Regassa LB. Staphylococcal enterotoxins, toxic shock syndrome toxin and streptococcal pyrogenic exotoxins A comparative study of their molecular biology. Chem Immunol. 1992 55 1-35. [Pg.629]

Tsao N, Tsai 0, Lin YS et al. Streptococcal pyrogenic exotoxin B cleaves properdin and inhibits complement-mediated opsonophagocytosis. Biochem Biophys Res Commun 2006 339(3) 779-784. [Pg.45]

Kuo CF, Lin YS, Chuang WJ et al. Degrading Complement 3 by Streptococcal Pyrogenic Exotoxin B Inhibits Complement Activation and Neutrophil Opsonophagocytosis. Infect Immun 2008 76(3) 1116-1169. [Pg.45]

Colon-Whitt A., Whitt R.S., Cole R.M. 1979. Production of an erythrogenic toxin (streptococcal pyrogenic exotoxin) by a nonlysogenized group A streptococcus. In Pathogenic streptococci, (Ed Parker, M.T.) Reedbooks, England, 64-65. [Pg.150]

Goshom, S.C. and Schlievert, P.M. 1988. Nucleotide sequence of streptococcal pyrogenic exotoxin type C. [Pg.151]

Hauser, A.R., Vath, G.M., Ohlendorf, D.H., and Schlievert, P.M. 1995. Structural studies of streptococcal pyrogenic exotoxin superantigens. In Bacterial Superantigens Structure. Function and Therapeutic Potential. (Eds Thibodeau, J. and Sekaly, R.P.) Springer-Verlag, New York, 39-48. [Pg.151]

Johnson, L.P., Schlievert, P.M., and Watson, D.W. 1980. Transfer of group A streptococcal pyrogenic exotoxin production to non-toxigenic strains by lysogenic conversion. Infect. Immun. 28 254-257. [Pg.152]


See other pages where Pyrogens streptococcal exotoxins is mentioned: [Pg.3053]    [Pg.5132]    [Pg.273]    [Pg.5]    [Pg.20]    [Pg.86]    [Pg.163]    [Pg.5131]    [Pg.623]    [Pg.689]    [Pg.132]    [Pg.132]    [Pg.138]    [Pg.152]   
See also in sourсe #XX -- [ Pg.3053 ]




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