Structure of the transmembrane domain of HIV-1 envelope glycoprotein.
Structure of the transmembrane domain of HIV-1 envelope glycoprotein.
复制标题
DOI：
10.1111/febs.13954
复制
发表时间：
2017-04
期刊：
影响因子：
--
通讯作者：
Chou JJ
中科院分区：
文献类型：
--
作者：
Chen B;Chou JJ
HIV-1 包膜刺突 (Env) 是一种高度糖基化的 I 型膜蛋白，可介导病毒和细胞膜的融合以引发感染。它也是中和抗体的主要目标，因此是疫苗开发的重要候选者。我们最近报道了在类膜环境中重建的 HIV-1 Env 跨膜 (TM) 结构域的 NMR 结构。以 HIV-1 为例，我们在此讨论 TM 结构域如何锚定、稳定和调节病毒包膜刺突，以及其高分辨率结构如何有助于理解病毒膜融合和免疫原设计。
HIV-1 envelope spike (Env) is a heavily glycosylated, type I membrane protein that mediates fusion of viral and cell membranes to initiate infection. It is also a primary target of neutralizing antibodies and thus an important candidate for vaccine development. We have recently reported an NMR structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in a membrane-like environment. Taking HIV-1 as an example, we discuss here how a TM domain can anchor, stabilize and modulate a viral envelope spike and how its high-resolution structure can contribute to understanding viral membrane fusion and to immunogen design.