The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction
The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction
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DOI：
10.1016/j.str.2013.05.018
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发表时间：
2013-08-06
期刊：
影响因子：
5.7
通讯作者：
Gruenewald, Kay
中科院分区：
文献类型：
--
作者：
Maurer, Ulrike E.;Zeev-Ben-Mordehai, Tzviya;Gruenewald, Kay
糖蛋白B（gB）是复杂疱疹病毒融合机制的关键组分。我们研究了两个gB胞外域形式的膜相互作用，并提出了一个电子cryotomography结构的gB-双层复合物。这两种形式在存在或不存在膜近端区域（MPR）方面不同，但显示出总体相似的三聚体形状。MPR的存在阻碍了与脂质体的相互作用。相比之下，MPR缺乏形式有效地与脂质体相互作用。横向相互作用导致在膜上形成涂层。结构表明，gB与膜的相互作用是由融合环介导的，并限于外膜小叶。所观察到的固有倾向的gB集群的膜上表明的额外的作用，gB在推动融合过程中向前超越瞬时融合孔开放，并随后导致融合孔扩张。
Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion.