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Titolo:
The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant
Autore:
Losman, B; Biller, M; Olofsson, S; Schonning, K; Lund, OS; Svennerholm, B; Hansen, JES; Bolmstedt, A;
Indirizzi:
Gothenburg Univ, Dept Clin Virol, S-41346 Gothenburg, Sweden Gothenburg Univ Gothenburg Sweden S-41346 ol, S-41346 Gothenburg, Sweden Univ Copenhagen, Hvidovre Hosp, Dept Infect Dis 144, DK-2650 Hvidovre, Denmark Univ Copenhagen Hvidovre Denmark DK-2650 144, DK-2650 Hvidovre, Denmark
Titolo Testata:
FEBS LETTERS
fascicolo: 1-2, volume: 454, anno: 1999,
pagine: 47 - 52
SICI:
0014-5793(19990702)454:1-2<47:TNGOTV>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUTRALIZATION SENSITIVITY; ENVELOPE GLYCOPROTEIN; CARBOHYDRATE EPITOPES; SYNCYTIUM FORMATION; MACROPHAGE TROPISM; SYNTHETIC PEPTIDES; ANTIBODIES; LOOP; INFECTION; FUSION;
Keywords:
acquired immunodeficiency syndrome; U937; macrophage; human immunodeficiency virus type 1; carbohydrate;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Bolmstedt, A Gothenburg Univ, Dept Clin Virol, Guldhedsgatan 10B, S-41346 Gothenburg, Sweden Gothenburg Univ Guldhedsgatan 10B Gothenburg Sweden S-41346
Citazione:
B. Losman et al., "The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant", FEBS LETTER, 454(1-2), 1999, pp. 47-52

Abstract

We have previously shown that an N-glycosylation site of N306 of HIV-1 gp120 is not necessary for the HIV-1 infectivity but protects HIV-1 from neutralising antibodies, In contrast Nakayama et al, FEES Lett, (1998) 426, 367-372], using a virus with an identical V3 region, suggested that eliminationof this particular glycan reduced the ability of T-tropic HIV to bind to CXCR4 and hence its ability to infect T cell lines, We therefore re-examinedthe ability of a mutant virus, lacking the N306 glycan, to replicate in various types of cells and found no change in co-receptor usage for mutant virus. The ability of mutant virus to replicate or to induce syncytia in infected cells was similar to that of wild type virus. These results corroborate our original observation, confirming that the induced mutation in the N306 glycosylation site neither impairs nor improves the ability of mutant virus to replicate in permissive cells. (C) 1999 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 23:57:07