Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1)Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1)
SPEC_STRP8 Superantigen that acts as a causative agent of the symptoms associated with scarlet fever (PubMed:1500157, PubMed:1987034, PubMed:9253413, PubMed:11163233). Has been associated with streptococcal toxic shock-like disease and may play a role in the early events of rheumatic fever (PubMed:1500157, PubMed:9253413, PubMed:11163233). Superantigens cross-link major histocompatibility complex (MHC) class II and T-cell receptor (TCR) molecules, resulting in an overstimulation of T-cells associated with a massive release of pyrogenic and inflammatory cytokines (PubMed:9253413, PubMed:11163233).[1][2][3][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Li Y, Li H, Dimasi N, McCormick JK, Martin R, Schuck P, Schlievert PM, Mariuzza RA. Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II. Immunity. 2001 Jan;14(1):93-104. PMID:11163233
↑Kapur V, Nelson K, Schlievert PM, Selander RK, Musser JM. Molecular population genetic evidence of horizontal spread of two alleles of the pyrogenic exotoxin C gene (speC) among pathogenic clones of Streptococcus pyogenes. Infect Immun. 1992 Sep;60(9):3513-7. PMID:1500157 doi:10.1128/iai.60.9.3513-3517.1992
↑Yu CE, Ferretti JJ. Frequency of the erythrogenic toxin B and C genes (speB and speC) among clinical isolates of group A streptococci. Infect Immun. 1991 Jan;59(1):211-5. PMID:1987034 doi:10.1128/iai.59.1.211-215.1991
↑Roussel 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. 1997 Aug;4(8):635-43. PMID:9253413
