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
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
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DOI：
10.1128/jvi.72.3.2500-2504.1998
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发表时间：
1998-03-01
影响因子：
5.4
通讯作者：
Gorny, MK
中科院分区：
文献类型：
--
作者：
Bandres, JC;Wang, QF;Gorny, MK
趋化因子受体CXCR 4（也称为LESTR和融合蛋白）已被证明是人类免疫缺陷病毒1型（HIV-1）嗜T细胞株的辅助受体。我们已经开发了一种结合试验，表明HIV包膜（Env）可以与CXCR 4相互作用，而不依赖于CD 4，但这种结合明显增强了珍贵的相互作用Env与可溶性CD 4。我们还发现，非糖基化的HIV-1（SF-2）gp 120或偏高碘酸钠处理的HIV-1（451）寡聚体gp 160比具有完整碳水化合物残基的对应物更容易与CXCR 4结合。
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.