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Titolo:
RESISTANCE TO V3-DIRECTED NEUTRALIZATION CAUSED BY AN N-LINKED OLIGOSACCHARIDE DEPENDS ON THE QUATERNARY STRUCTURE OF THE HIV-1 ENVELOPE OLIGOMER
Autore:
SCHONNING K; JANSSON B; OLOFSSON S; NIELSEN JO; HANSEN JES;
Indirizzi:
HVIDOVRE UNIV HOSP,DEPT 144,INFECT DIS LAB,KETTEGARD ALLE 30 DK-2650 HVIDOVRE DENMARK HVIDOVRE UNIV HOSP,DEPT 144,INFECT DIS LAB DK-2650 HVIDOVRE DENMARK GOTHENBURG UNIV,DEPT CLIN VIROL S-41346 GOTHENBURG SWEDEN
Titolo Testata:
Virology
fascicolo: 1, volume: 218, anno: 1996,
pagine: 134 - 140
SICI:
0042-6822(1996)218:1<134:RTVNCB>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; SOLUBLE CD4; IMMUNOSORBENT-ASSAY; LOWER AFFINITY; GLYCOPROTEIN; ANTIBODIES; GP120; GP41; TRANSPORT; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
K. Schonning et al., "RESISTANCE TO V3-DIRECTED NEUTRALIZATION CAUSED BY AN N-LINKED OLIGOSACCHARIDE DEPENDS ON THE QUATERNARY STRUCTURE OF THE HIV-1 ENVELOPE OLIGOMER", Virology, 218(1), 1996, pp. 134-140

Abstract

A conserved N-glycan present within the V3 loop of gp120 modulates the sensitivity to neutralization by antibodies directed to the Vs loop. A glycan-deficient mutant of HIVLAI, designated HIVA308, displayed a 100-fold increase in sensitivity to neutralization by anti-V3 MAb NEA-9205 compared to wild-type HIVLAI. This difference in sensitivity was not caused by an alteration of the antibody binding site itself, as NEA-9205 had equal affinity for both wild-type and mutant monomeric gp120, In contrast, virion-associated wild-type gp120 was immunoprecipitated less efficiently with NEA-9205 than virion-associated mutant gp120. This difference was completely abrogated, if immunoprecipitation werecarried out in the presence of detergent. Furthermore, treatment of virion preparations with detergent exposed the C-terminal D7324 epitope, which is inaccessible on virion-associated gp120 but readily accessible on monomeric, soluble gp120. Finally, both wild-type and mutant monomeric, soluble gp120 were precipitated equally efficiently by NEA-9205 in the absence of detergent. Thus, the NEA-9205 epitope was readilyaccessible on monomeric gp120 regardless of the presence of the N-306-glycan, and inaccessibility of the NEA-9205 epitope imparted by the N-306-glycan was observed only on the intact envelope oligomer. (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 05:13:27