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Titolo:
CONSERVED N-LINKED OLIGOSACCHARIDES OF THE C-TERMINAL PORTION OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GP120 AND VIRAL SUSCEPTIBILITY TO NEUTRALIZING ANTIBODIES
Autore:
HEMMING A; GRAM GJ; BOLMSTEDT A; LOSMAN B; HANSEN JES; RICKSTEN A; OLOFSSON S;
Indirizzi:
GOTHENBURG UNIV,DEPT CHEM VIROL,GULDHEDSGATAN 10B S-41346 GOTHENBURG SWEDEN GOTHENBURG UNIV,DEPT CLIN VIROL S-41346 GOTHENBURG SWEDEN INFECT DIS LAB HVIDOVRE DENMARK
Titolo Testata:
Archives of virology
fascicolo: 11, volume: 141, anno: 1996,
pagine: 2139 - 2151
SICI:
0304-8608(1996)141:11<2139:CNOOTC>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENVELOPE GLYCOPROTEIN GP120; HUMAN MONOCLONAL-ANTIBODIES; SURFACE GLYCOPROTEIN; GLYCOSYLATION SITES; DISULFIDE BONDS; FUSION ACTIVITY; HIV-1 GP120; CD4 BINDING; REGION; EPITOPES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
A. Hemming et al., "CONSERVED N-LINKED OLIGOSACCHARIDES OF THE C-TERMINAL PORTION OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GP120 AND VIRAL SUSCEPTIBILITY TO NEUTRALIZING ANTIBODIES", Archives of virology, 141(11), 1996, pp. 2139-2151

Abstract

We have constructed a mutated infectious HIV variant lacking the signals for addition of three N-linked glycans situated in the V4, C4 and V5 regions of HIV gp120. When comparing mutated virus with wildtype virus we found essentially no differences in the phenotypic characteristics of the two viruses except for the expected electrophoretic mobility shift of radioimmuno-precipitated mutated gp120, resulting from the missing N-glycans. Thus, the infectivity titer and the capacity to induce syncytia were similar for the two viruses. The sensitivity of mutant and wildtype virus to a number of neutralizing agents was determined. As expected, the mutant virus was significantly less sensitive to neutralization by Con A, with affinity for the N-glycans eliminated. Wefound, however, that antibodies to the V3 loop and sCD4 neutralized wild-type virus as efficiently as mutant virus, whereas 2G12, a monoclonal antibody, binding to a discontinuous neutralization epitope, and GP13, binding to the CD4-binding domain, neutralized wildtype virus better than mutant virus. Altogether the data suggest that the three conserved N-linked glycans, despite their location in immediate association with the CD4-binding domain, which is an important neutralization epitope, are not essential for virus replication in cell culture and they are not engaged in shielding neutralization epitopes of gp120 from neutralizing antibodies. However, the glycans evidently influence the three-dimensional conformation of gp120, since their presence increasesthe availability of the neutralization epitope of 2G12.

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Documento generato il 24/11/20 alle ore 14:17:03