Lab, of Molecular Biology and Viral Oncogenesis & AIDS Reference Center, Istituto Nazionale Tumori Fond, G, Pascale, Naples, Italy.
J Transl Med. 2011 Jan 27;9 Suppl 1(Suppl 1):S1. doi: 10.1186/1479-5876-9-S1-S1.
The human immunodeficiency virus type 1 (HIV-1) external envelope glycoprotein gp120 presents conserved binding sites for binding to the primary virus receptor CD4 as well as the major HIV chemokine coreceptors, CCR5 and CXCR4. Concerted efforts are underway to understand the specific interactions between gp120 and coreceptors as well as their contribution to the subsequent membrane fusion process. The present review summarizes the current knowledge on this biological aspect, which represents one of the key and essential points of the HIV-host cell interplay and HIV life cycle. The relevance of conformational HIV-1 Envelope proteins presented on Virus-like Particles for appropriate assessment of this molecular interaction, is also discussed.
人类免疫缺陷病毒 1 型（HIV-1）的外膜糖蛋白 gp120 呈现出与主要病毒受体 CD4 以及主要 HIV 趋化因子受体 CCR5 和 CXCR4 结合的保守结合位点。目前正在共同努力了解 gp120 与核心受体之间的特定相互作用及其对随后的膜融合过程的贡献。本综述总结了关于这一生物学方面的现有知识，这是 HIV-宿主细胞相互作用和 HIV 生命周期的关键和基本要点之一。还讨论了病毒样颗粒上呈现的构象 HIV-1 包膜蛋白对于适当评估这种分子相互作用的相关性。
