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Titolo:
INHIBITION OF ANTIGEN-SPECIFIC T-CELL ACTIVATION BY STAPHYLOCOCCAL ENTEROTOXINS
Autore:
DOWD JE; JENKINS RN; KARP DR;
Indirizzi:
UNIV TEXAS,SW MED CTR,SIMMONS ARTHRIT RES CTR,5323 HARRY HINES BLVD DALLAS TX 75235 UNIV TEXAS,SW MED CTR,SIMMONS ARTHRIT RES CTR DALLAS TX 75235
Titolo Testata:
The Journal of immunology
fascicolo: 3, volume: 154, anno: 1995,
pagine: 1024 - 1031
SICI:
0022-1767(1995)154:3<1024:IOATAB>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLASS-II MOLECULES; AUREUS TOXIN SUPERANTIGENS; SHOCK SYNDROME TOXIN-1; RECEPTOR BETA-CHAIN; HLA-DR; VARIABLE REGION; BINDING; PEPTIDES; IDENTIFICATION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
J.E. Dowd et al., "INHIBITION OF ANTIGEN-SPECIFIC T-CELL ACTIVATION BY STAPHYLOCOCCAL ENTEROTOXINS", The Journal of immunology, 154(3), 1995, pp. 1024-1031

Abstract

The staphylococcal enterotoxins SEA, SEE, SEC(2), and TSST-1 bind to MHC class II molecules and stimulate polyclonal T cell populations on the basis of the expression of responsive TCR V beta domains. CL-1 is a human T cell clone that is specific for a peptide derived from influenza hemagglutinin (HA 307-319) presented in the context of HLA-DR1. CL-1 expresses the TCR V beta 13.1 domain, and does not respond to SEA,SEE, or TSST-1. This T cell was used to test the effect of nonstimulatory staphylococcal enterotoxins on a response to antigenic peptide. These toxins inhibit peptide-specific activation of CL-1 in a concentration-dependent manner. These toxins also inhibit the response of an HLA-DR1-specific alloreactive T cell clone. This inhibition seems to be a result of impaired access of TCR to the MHC/peptide complex rather than negative signaling by toxin via class II interaction or induction of T cell anergy. SEA, but neither SEB nor TSST-1 impedes avidin access to a biotin group attached to the amino terminus of HA 307-319. SEA partially impairs access of avidin to HA peptide biotinylated at residue 313, but is unable to inhibit avidin access to biotin at residue 318. This demonstrates that SEA binds to HLA-DR molecules that have alsobound the antigenic peptide and suggests a topology for the interaction of SEA with class II, whereby the toxin interferes with peptide/MHC-TCR contact.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 00:30:09