Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
HIV-1-INDUCED CELL-FUSION IS MEDIATED BY MULTIPLE REGIONS WITHIN BOTHTHE VIRAL ENVELOPE AND THE CCR-5 CORECEPTOR
Autore:
BIENIASZ PD; FRIDELL RA; ARAMORI I; FERGUSON SSG; CARON MG; CULLEN BR;
Indirizzi:
DUKE UNIV,MED CTR,HOWARD HUGHES MED INST DURHAM NC 27710 DUKE UNIV,MED CTR,HOWARD HUGHES MED INST DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT GENET DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT CELL BIOL DURHAM NC 27710
Titolo Testata:
EMBO journal
fascicolo: 10, volume: 16, anno: 1997,
pagine: 2599 - 2609
SICI:
0261-4189(1997)16:10<2599:HCIMBM>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; MONONUCLEAR PHAGOCYTES; V3 LOOP; TROPISM; HIV-1; DETERMINANT; INFECTION; TYPE-1; IDENTIFICATION; GP120;
Keywords:
CHEMOKINE RECEPTORS; HIV-1 CO-RECEPTORS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
P.D. Bieniasz et al., "HIV-1-INDUCED CELL-FUSION IS MEDIATED BY MULTIPLE REGIONS WITHIN BOTHTHE VIRAL ENVELOPE AND THE CCR-5 CORECEPTOR", EMBO journal, 16(10), 1997, pp. 2599-2609

Abstract

Although the human hCCR-5 chemokine receptor can serve as a co-receptor for both M-tropic (ADA and Bat) and dual-tropic (89.6) strains of human immunodeficiency virus type 1 (HIV-1), the closely related mouse mCCR-5 homolog is inactive, We used chimeric hCCR-5-mCCR-5 receptor molecules to examine the functional importance of the three extracellular domains of hCCR-5 that differ in sequence from their mCCR-5 equivalents, While this analysis revealed that all three of these extracellular domains could participate in the functional interaction with HIV-1 envelope, clear differences were observed when different HIV-1 strains were analyzed. Thus, while the ADA HIV-1 isolate could effectively utilize chimeric human-mouse CCR-5 chimeras containing any single human extracellular domain, the Bat isolate required any two human extracellular sequences while the 89.6 isolate would only interact effectively with chimeras containing all three human extracellular sequences. Further analysis using hybrid HIV-1 envelope proteins showed that the difference in co-receptor specificity displayed by the ADA and Bat isolateswas due partly to a single amino acid change in the V3 loop, althoughthis interaction was clearly also modulated by other envelope domains, Overall, these data indicate that the interaction between HIV-1 envelope and CCR-5 is not only complex but also subject to marked, HIV-1 isolate-dependent variation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 17:48:40