Human immunodeficiency virus (HIV) envelope binds to CXCR4 independently of CD4, and binding can be enhanced by interaction with soluble CD4 or by HIV envelope deglycosylation

被引:91
作者
Bandres, JC
Wang, QF
O'Leary, J
Baleaux, F
Amara, A
Hoxie, JA
Zolla-Pazner, S
Gorny, MK
机构
[1] Manhattan VA Med Ctr, Res Ctr AIDS & HIV Infect, New York, NY 10010 USA
[2] NYU, Dept Pathol, New York, NY 10010 USA
[3] NYU, Dept Med, New York, NY 10010 USA
[4] Inst Pasteur, Unite Immunol Virale, F-75724 Paris 15, France
[5] Univ Penn, Div Hematol Oncol, Philadelphia, PA 19104 USA
关键词
D O I
10.1128/JVI.72.3.2500-2504.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Chemokine receptor CXCR4 (also known as LESTR and fusin) has been shown to function as a coreceptor for T-cell-tropic strains of human immunodeficiency virus type 1 (HIV-1). We have developed a binding assay to show that HIV envelope (Env) can interact with CXCR4 independently of CD4 but that this binding is markedly enhanced by the precious interaction of Env with soluble CD4. We also show that nonglycosylated HIV-1(SF-2) gp120 or sodium metaperiodate-treated oligomeric gp160 from HIV-1(451) bound much more readily to CXCR4 than their counterparts with intact carbohydrate residues did.
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收藏
页码:2500 / 2504
页数:5
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