Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein.
Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein.
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人类免疫缺陷病毒1型gp120包膜糖蛋白与gp41跨膜糖蛋白的相互作用分析。
DOI：
10.1128/jvi.71.12.9722-9731.1997
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发表时间：
1997
影响因子：
5.4
通讯作者：
Sodroski,J
中科院分区：
文献类型：
--
作者：
Wyatt,R;Desjardin,E;Olshevsky,U;Nixon,C;Binley,J;Olshevsky,V;Sodroski,J
人类免疫缺陷病毒1型(HIV-1)gp120外膜糖蛋白与病毒受体(CD4)和gp41跨膜糖蛋白相互作用。为了研究gp120和gp41包膜糖蛋白之间的相互作用，我们比较了抗gp120单抗与含有gp120和gp41外区的可溶性糖蛋白sgp140的结合能力。后一种分子上gp120表位的一个子集的封闭或改变允许在gp120抗体竞争图上定义gp41“足迹”。这些表位对sgp140糖蛋白的封闭作用通过与可溶性CD4的结合而减少。与gp41胞外区相互作用的gp120表位被第一个(C1)和第五个(C5)保守的gp120区的缺失所破坏。这些缺失不影响与CD4和中和性单抗的不连续结合部位的完整性。因此，引起非中和抗体的HIV-1gp120糖蛋白上的gp41界面可以被移除，同时保留免疫上理想的gp120结构。
The human immunodeficiency virus type 1 (HIV-1) gp120 exterior envelope glycoprotein interacts with the viral receptor (CD4) and with the gp41 transmembrane envelope glycoprotein. To study the interaction of the gp120 and gp41 envelope glycoproteins, we compared the abilities of anti-gp120 monoclonal antibodies to bind soluble gp120 and a soluble glycoprotein, sgp140, that contains gp120 and gp41 exterior domains. The occlusion or alteration of a subset of gp120 epitopes on the latter molecule allowed the definition of a gp41 "footprint" on the gp120 antibody competition map. The occlusion of these epitopes on the sgp140 glycoprotein was decreased by the binding of soluble CD4. The gp120 epitopes implicated in the interaction with the gp41 ectodomain were disrupted by deletions of the first (C1) and fifth (C5) conserved gp120 regions. These deletions did not affect the integrity of the discontinuous binding sites for CD4 and neutralizing monoclonal antibodies. Thus, the gp41 interface on the HIV-1 gp120 glycoprotein, which elicits nonneutralizing antibodies, can be removed while retaining immunologically desirable gp120 structures.