Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
Biochim Biophys Acta Biomembr. 2017 Apr;1859(4):550-560. doi: 10.1016/j.bbamem.2016.10.012. Epub 2016 Oct 25.
The HIV gp160 envelope fusion protein is situated in the viral membrane and mediates virus entry into its host cell. Increasing evidence suggests that virtually all parts of the HIV envelope are structurally and functionally dependent on membranes. Protein-lipid interactions and membrane properties influence the dynamics of a manifold of gp160 biological activities such as membrane fusion, immune suppression and gp160 incorporation into virions during HIV budding and assembly. In the following we will summarize our current understanding of this interdependence between membrane interaction, structural conformation and functionality of the different gp160 domains. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.
HIV gp160 包膜融合蛋白位于病毒膜上,并介导病毒进入宿主细胞。越来越多的证据表明,HIV 包膜的几乎所有部分在结构和功能上都依赖于膜。蛋白质-脂质相互作用和膜特性影响 gp160 的多种生物学活性的动力学,如膜融合、免疫抑制和 HIV 出芽和组装过程中 gp160 掺入病毒粒子。在下面,我们将总结我们目前对不同 gp160 结构域的膜相互作用、结构构象和功能之间这种相互依赖性的理解。本文是由 Dirk Schneider 编辑的题为“脂质有序/脂质缺陷和脂质对蛋白质活性的控制”的特刊的一部分。