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Titolo:
Characterization of the interaction of a TCR alpha chain variable domain with MHC II I-A molecules
Autore:
Qadri, A; Thatte, J; Radu, CG; Ober, B; Ward, ES;
Indirizzi:
Univ Texas, SW Med Ctr, Ctr Immunol, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 Med Ctr, Ctr Immunol, Dallas, TX 75235 USA Univ Texas, SW Med Ctr, Ctr Canc Immunobiol, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 Ctr Canc Immunobiol, Dallas, TX 75235 USA
Titolo Testata:
INTERNATIONAL IMMUNOLOGY
fascicolo: 6, volume: 11, anno: 1999,
pagine: 967 - 977
SICI:
0953-8178(199906)11:6<967:COTIOA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-CELL-RECEPTOR; MAJOR HISTOCOMPATIBILITY COMPLEX; MYELIN BASIC-PROTEIN; CRYSTAL-STRUCTURE; 3-DIMENSIONAL STRUCTURE; ANTIGEN RECEPTOR; BETA-CHAIN; AUTOIMMUNE ENCEPHALOMYELITIS; PROCESSING PATHWAYS; INTACT PROTEINS;
Keywords:
fourth hypervariable region; immunosuppression; MHC class II; TCR; V-alpha domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
69
Recensione:
Indirizzi per estratti:
Indirizzo: Ward, ES Univ Texas, SW Med Ctr, Ctr Immunol, 5323 Harry Hines Blvd, Dallas, TX 75235 USA Univ Texas 5323 Harry Hines Blvd Dallas TX USA 75235 TX 75235 USA
Citazione:
A. Qadri et al., "Characterization of the interaction of a TCR alpha chain variable domain with MHC II I-A molecules", INT IMMUNOL, 11(6), 1999, pp. 967-977

Abstract

The ap TCR recognizes peptides bound to MHC molecules. In the present study, we analyzed the interaction of a soluble TCR a chain variable domain (V(alpha)4.2-J(alpha)40; abbreviated to V(alpha)4.2) with the MHC class II molecule I-AU. V-alpha,4.2 bound specifically to I-AU expressed on the surfaceof a transfected thymoma cell line. Modifications in the amino acid residues located within the three complementarity-determining regions (CDRs) of the V alpha, domain did not markedly affect this interaction. However, mutation of glutamic acid to alanine at position 69 of the fourth hypervariable region (HV4 alpha) significantly increased the binding. Antibody inhibitionstudies suggested that the binding site was partly contributed by a regionof the beta chain of I-A(u). Furthermore, the binding of V(alpha)4.2 to the MHC molecule was dependent on the nature of the peptide bound in the groove. Soluble V(alpha)4.2 specifically inhibited the activation of TCR transfectants by I-Au-expressing cells pulsed with an N-terminal peptide of myelin basic protein. V(alpha)4.2 also bound to MHC class II-expressing spleen cell populations from mice of the H-2(U) and H-2(d) haplotypes, The binding of V(alpha)4.2 to I-A molecules might explain the immunoregulatory effects reported previously for TCR a chains. This V(alpha)4.2 interaction may alsobe relevant to models of antigen presentation involving the binding of intact proteins to MHC class II molecules followed by their processing to generate epitopes suitable for T cell recognition.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 14:37:48