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Titolo:
Envelope glycoprotein determinants of neutralization resistance in a simian-human immunodeficiency virus (SHIV-HXBc2P 3.2) derived by passage in monkeys
Autore:
Si, ZH; Cayabyab, M; Sodroski, J;
Indirizzi:
Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Pathol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 Inst, Dept Pathol, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Canc Immunol & AIDS, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 anc Immunol & AIDS, Boston, MA 02115 USA Harvard Univ, Sch Publ Hlth, Dept Immunol & Infect Dis, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 munol & Infect Dis, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 9, volume: 75, anno: 2001,
pagine: 4208 - 4218
SICI:
0022-538X(200105)75:9<4208:EGDONR>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN MONOCLONAL-ANTIBODY; T-LYMPHOTROPIC RETROVIRUS; AMINO-ACID SUBSTITUTIONS; RECOMBINANT SOLUBLE CD4; N-LINKED GLYCOSYLATION; PIG-TAILED MACAQUES; AIDS-LIKE DISEASE; IN-VIVO; TRANSMEMBRANE PROTEIN; PERSISTENT INFECTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
89
Recensione:
Indirizzi per estratti:
Indirizzo: Sodroski, J Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Pathol, 44 Binney St,JFB 824, Boston, MA 02115 USA Harvard Univ 44 Binney St,JFB 824 Boston MA USA 02115 2115 USA
Citazione:
Z.H. Si et al., "Envelope glycoprotein determinants of neutralization resistance in a simian-human immunodeficiency virus (SHIV-HXBc2P 3.2) derived by passage in monkeys", J VIROLOGY, 75(9), 2001, pp. 4208-4218

Abstract

The simian-human immunodeficieny virus SHIV-HXBc2 contains the envelope glycoproteins of a laboratory-adapted, neutralization-sensitive human immunodeficiency virus type 1 variant, HXBc2. Serial in vivo passage of the nonpathogenic SHIV7-HXBc2 generated SHIV KU-1, which causes rapid CD4(+) T-cell depletion and an AIDS-Iike illness in monkeys, A molecularly cloned pathogenic SHIV, SHIV-HXBc2P 3.2? was derived from the SHIV KU-1 isolate and differs from the parental SHIV-HXBc2 by only 12 envelope glycoprotein amino acid residues. Relative to SHIV-HXBc2, SHIV-HXBc2P 3.2 was resistant to neutralization by all of the antibodies tested with the exception of the 2G12 antibody. The sequence changes responsible for neutralization resistance were located in variable regions of the gp120 exterior envelope glycoprotein and in the gp-ll transmembrane envelope glycoprotein. The 2G12 antibody, which neutralized SHIV-HXBc2 and SHIV-HXBc2P 3.2 equally, bound the HXBc2 and HXBc2P 3,2 envelope glycoproteins on the cell surface comparably. The ability of the other tested antibodies to achieve saturation was less for the HXBc2P3.2 envelope glycoproteins than for the HXBc2 envelope glycoproteins. eventhough the affinity of the antibodies for the two envelope glycoproteins was similar, Thus, a highly neutralization sensitive SHIV, by modifying bothgp120 and gp41 glycoproteins, apparently achieves a neutralization-resistant state by decreasing the saturability of its envelope glycoproteins by antibodies.

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Documento generato il 29/11/20 alle ore 00:28:16