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Titolo:
N-LINKED GLYCANS IN THE CD4-BINDING DOMAIN OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEIN GP160 ARE ESSENTIAL FOR THE IN-VIVOPRIMING OF T-CELLS RECOGNIZING AN EPITOPE LOCATED IN THEIR VICINITY
Autore:
SJOLANDER S; BOLMSTEDT A; AKERBLOM L; HORAL P; OLOFSSON S; MOREIN B; SJOLANDER A;
Indirizzi:
SWEDISH UNIV AGR SCI,BIOMEDICUM,COLL VET MED,DEPT VET MICROBIOL,SECT VIROL,BOX 585 S-75123 UPPSALA SWEDEN GOTHENBURG UNIV,DEPT CLIN VIROL S-41346 GOTHENBURG SWEDEN NATL VET INST,DEPT VIROL,BIOMEDICUM S-75123 UPPSALA SWEDEN
Titolo Testata:
Virology
fascicolo: 2, volume: 215, anno: 1996,
pagine: 124 - 133
SICI:
0042-6822(1996)215:2<124:NGITCD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
CROSS-NEUTRALIZING ANTIBODIES; MAJOR HISTOCOMPATIBILITY COMPLEX; HUMAN MONOCLONAL-ANTIBODY; SYNTHETIC PEPTIDES; INFLUENZA HEMAGGLUTININ; GLYCOSYLATION SITES; RECOMBINANT GP160; RECEPTOR-BINDING; DISULFIDE BONDS; MHC MOLECULES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
63
Recensione:
Indirizzi per estratti:
Citazione:
S. Sjolander et al., "N-LINKED GLYCANS IN THE CD4-BINDING DOMAIN OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEIN GP160 ARE ESSENTIAL FOR THE IN-VIVOPRIMING OF T-CELLS RECOGNIZING AN EPITOPE LOCATED IN THEIR VICINITY", Virology, 215(2), 1996, pp. 124-133

Abstract

Deglycosylation of viral glycoproteins has been suggested to influence the number of available T cell determinants and to increase T cell recognition of antigens. In this study, we have investigated whether T cell responses to the HIV-I envelope glycoprotein gp160 were influenced by deletion of three N-glycans of the protein. Wild type (wt) and a mutated form of gp160 (gp160(A123)) lacking the three N-glycans in theC-terminal CD4-binding region efficiently induced antigen-specific T cell responses in mice of the H-2(b), H-2(d), and H-2(k) haplotypes. Further, T cells primed by either wt gp160 or gp160(A123) were stimulated in vitro to a similar extent by the homologous and heterologous protein, indicating that deletion of the glycans did not affect the overall immunogenicity and antigenicity of gp160(A123). Wild-type gp160 andgp160(A123) induced comparable T cell responses to those of epitopes which with respect to the secondary structure of gp160 were distant from the deleted glycans. However, in mice of the H-2(b) haplotype, wt gp160 primed T cells which responded in vitro to a peptide containing one of the deleted N-glycosylation sites (Asn(448)), whereas T cells induced by gp160(A123) were unable to recognize this peptide. Thus, deletion of the glycans abrogated the in vivo priming of T cells recognizing an epitope in close proximity to the deletion sites. Furthermore, enzymatically deglycosylated gp160 failed to induce a T cell response to this epitope. These results indicate that the in vivo generation of certain T cell determinants from glycoproteins is dependent on the glycosylation of the protein. (C) 1996 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 05:39:21