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人类免疫缺陷病毒(HIV)包膜可独立于CD4与CXCR4结合,与可溶性CD4相互作用或HIV包膜去糖基化可增强这种结合。

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.

作者信息

Bandres J C, Wang Q F, O'Leary J, Baleaux F, Amara A, Hoxie J A, Zolla-Pazner S, Gorny M K

机构信息

Research Center for AIDS and HIV Infection, Manhattan VA Medical Center, and Department of Pathology, New York University, New York 10010, USA.

出版信息

J Virol. 1998 Mar;72(3):2500-4. doi: 10.1128/JVI.72.3.2500-2504.1998.

Abstract

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 previous 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.

摘要

趋化因子受体CXCR4(也称为LESTR和融合素)已被证明可作为1型人类免疫缺陷病毒(HIV-1)嗜T细胞株的共受体。我们开发了一种结合试验,以表明HIV包膜(Env)可独立于CD4与CXCR4相互作用,但Env与可溶性CD4的先前相互作用可显著增强这种结合。我们还表明,非糖基化的HIV-1(SF-2)gp120或经高碘酸钠处理的来自HIV-1(451)的寡聚gp160比具有完整碳水化合物残基的对应物更容易与CXCR4结合。

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