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Titolo:
Molecular function of the CD4 D1 domain in coreceptor-mediated entry by HIV type 1
Autore:
Esser, U; Speck, RF; Deen, KC; Atchison, RE; Sweet, R; Goldsmith, MA;
Indirizzi:
Gladstone Inst Virol & Immunol, San Francisco, CA 94141 USA Gladstone InstVirol & Immunol San Francisco CA USA 94141 o, CA 94141 USA SmithKline Beecham, King Of Prussia, PA 19046 USA SmithKline Beecham KingOf Prussia PA USA 19046 Of Prussia, PA 19046 USA Univ Calif San Francisco, Sch Med, Dept Med, San Francisco, CA 94141 USA Univ Calif San Francisco San Francisco CA USA 94141 ancisco, CA 94141 USA
Titolo Testata:
AIDS RESEARCH AND HUMAN RETROVIRUSES
fascicolo: 17, volume: 16, anno: 2000,
pagine: 1845 - 1854
SICI:
0889-2229(200011)16:17<1845:MFOTCD>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; GP120 ENVELOPE GLYCOPROTEIN; RECOMBINANT SOLUBLE CD4; T-CELL ACTIVATION; CD4-INDEPENDENT INFECTION; CHEMOKINE RECEPTORS; SYNCYTIUM FORMATION; STRUCTURAL-ANALYSIS; CDR3-LIKE REGION; AMINO-ACIDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Goldsmith, MA Univ Calif Davis, Ctr Comparat Med, Davis, CA 95616 USA UnivCalif Davis Davis CA USA 95616 ed, Davis, CA 95616 USA
Citazione:
U. Esser et al., "Molecular function of the CD4 D1 domain in coreceptor-mediated entry by HIV type 1", AIDS RES H, 16(17), 2000, pp. 1845-1854

Abstract

The surface molecule CD4 plays a key role in initiating cellular entry by the human immunodeficiency virus type 1 (HIV-1), and it is now recognized as acting synergistically with select chemokine receptors (coreceptors) in the infection process. The present study was undertaken to determine whetherthe extracellular region of CD4 is sufficient to induce fusion of HIV-1 virions with target cells in the absence of its anchoring function. Using pseudotype reporter viruses to quantitate infection, soluble CD4 (sCD4) was tested for its ability to induce fusion by viruses utilizing CCR5 as their coreceptor. We found that sCD4 was competent to replace membrane-bound CD4 totrigger infection mediated by several HIV-1 envelopes. Furthermore, in a comparison of the envelopes of HIV-1 NL4-3 and a chimera containing the gp120 V3 loop of Ba-L, the V3 region was found to be one factor affecting susceptibility to induction by sCD4. In addition, using truncated and mutant derivatives of sCD4, the amino-terminal D1 domain of CD4 was found to be necessary and sufficient for induction of fusion and to require an intact gp120-binding site for this activity. These results delineate determinants on CD4and gp120 required for fusion induction in collaboration with a coreceptor, and suggest a mechanism whereby CD4 may contribute to viral infection in trans.

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Documento generato il 30/11/20 alle ore 16:10:08