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Titolo:
SENSITIVITY OF HIV-1 TO NEUTRALIZATION BY ANTIBODIES AGAINST O-LINKEDCARBOHYDRATE EPITOPES DESPITE DELETION OF O-GLYCOSYLATION SIGNALS IN THE V3 LOOP
Autore:
HANSEN JES; JANSSON B; GRAM GJ; CLAUSEN H; NIELSEN JO; OLOFSSON S;
Indirizzi:
HVIDOVRE UNIV HOSP,LAB INFECT DIS 144 DK-2650 HVIDOVRE DENMARK GOTHENBURG UNIV,DEPT CLIN VIROL S-41124 GOTHENBURG SWEDEN UNIV COPENHAGEN,SCH DENT DK-1168 COPENHAGEN DENMARK
Titolo Testata:
Archives of virology
fascicolo: 2, volume: 141, anno: 1996,
pagine: 291 - 300
SICI:
0304-8608(1996)141:2<291:SOHTNB>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
J.E.S. Hansen et al., "SENSITIVITY OF HIV-1 TO NEUTRALIZATION BY ANTIBODIES AGAINST O-LINKEDCARBOHYDRATE EPITOPES DESPITE DELETION OF O-GLYCOSYLATION SIGNALS IN THE V3 LOOP", Archives of virology, 141(2), 1996, pp. 291-300

Abstract

It has been suggested that threonine or serine residues in the V3 loop of HIV-1 gp120 are glycosylated with the short-chain O-linked oligosaccharides Tn or sialosyl-Tn that function as epitopes for broadly neutralizing carbohydrate specific antibodies. In this study we examined whether mutation of such threonine or serine residues could decrease the sensitivity to infectivity inhibition by Tn or sialosyl-Tn specificantibodies. All potentially O-glycosylated threonine and serine residues in the V3 loop of cloned HIV-1(BRU) were mutagenized to alanine thus abrogating any O-glycosylation at these sites. Additionally, one ofthese T-A mutants (T308A) also abrogated the signal for N-glycosylation at N306 inside the V3-loop. The mutant clones were compared with the wild type virus as to sensitivity to neutralization with monoclonal and polyclonal antibodies specific for the tip of the V3 loop of BRU or for the O-linked oligosaccharides Tn or sialosyl-Tn. Deletion of theN-linked oligosaccharide at N306 increased the neutralization sensitivity to antibodies specific for the tip of the loop, which indicates that N-linked glycosylation modulates the accessibility to this immunodominant epitope. However, none of the mutants with deletions of O-glycosylation signals in the V3 loop displayed any decrease in sensitivityto anti-Tn or anti-sialosyl-Tn antibody. This indicates that these broadly specific neutralization epitopes are located outside the V3 loopof gp120.

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Documento generato il 04/12/20 alle ore 20:13:54