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Titolo:
V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCRS receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies
Autore:
Ly, A; Stamatatos, L;
Indirizzi:
Rockefeller Univ, Aaron Diamond AIDS Res Ctr, New York, NY 10016 USA Rockefeller Univ New York NY USA 10016 DS Res Ctr, New York, NY 10016 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 15, volume: 74, anno: 2000,
pagine: 6769 - 6776
SICI:
0022-538X(200008)74:15<6769:VLGOTH>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-CELL-LINE; HUMAN MONOCLONAL-ANTIBODY; MACROPHAGE TROPISM; V3 LOOP; SYNCYTIUM FORMATION; GLYCOPROTEIN GP120; LINKED OLIGOSACCHARIDES; SERUM NEUTRALIZATION; SEQUENCE CHANGES; N-GLYCOSYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Stamatatos, L Rockefeller Univ, Aaron Diamond AIDS Res Ctr, 455 1st Ave,7th Floor, New York, NY 10016 USA Rockefeller Univ 455 1st Ave,7th Floor New York NY USA 10016
Citazione:
A. Ly e L. Stamatatos, "V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCRS receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies", J VIROLOGY, 74(15), 2000, pp. 6769-6776

Abstract

examined the role of asparagine-linked glycosylation of the V2 loop of thehuman immunodeficiency virus (HIV) SF162 envelope on viral replication potential and neutralization susceptibility. We report that the asparagines located at the amino- and carboxy-terminal sites (at positions 154 and 195, respectively), as well as within the V2 loop of the SF162 envelope (at position 186), are glycosylated during in vitro replication of this virus in human peripheral blood mononuclear cells. Our studies indicate that glycosylation of the V2 loop, in particular at its base, facilitates the interaction of the HIV envelope with the CD4 and CCR5 receptor molecules present on thesurface of target cells and affects viral replication kinetics in a cell type-dependent manner. In cells expressing high numbers of receptor molecules on their surfaces, the SF162-derived V2 loop-deglycosylated mutant viruses replicate as efficiently as the parental SF162 virus, while in cells expressing small numbers of receptor molecules, the mutant viruses replicate with markedly reduced efficiency. In addition to expanding the viral tropism,V2 loop glycosylation at the three sites examined prevents neutralization by anti-CD4 binding site antibodies. In contrast, glycosylation at the amino- and carboxy-terminal sites of the V2 loop but not within the loop itselfoffers protection against anti-V3 loop antibodies. Thus, the epitopes masked by the sugar molecules present on the three glycosylation sites examinedare not identical but overlap.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 03:29:51