Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
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DOI：
10.1126/science.1127683
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发表时间：
2006-07-14
期刊：
影响因子：
56.9
通讯作者：
Gaudin, Yves
中科院分区：
文献类型：
--
作者：
Roche, Stephane;Bressanelli, Stephane;Gaudin, Yves
水泡性口炎病毒有一个非典型的膜融合糖蛋白(G)，在病毒表面的两种形式之间表现出依赖于pH的平衡。膜融合是在从高pH向低pH过渡的过程中触发的。低pH形式的G的结构在融合后的构象中显示了在所有其他融合蛋白中观察到的经典发夹构象，尽管有一种新的折叠结合了I类和II类融合蛋白的特征。这种结构为理解G构象变化的可逆性提供了一个框架。出乎意料的是，G与GB的疱疹病毒同源，这提出了关于病毒进化的重要问题。
The vesicular stomatitis virus has an atypical membrane fusion glycoprotein (G) exhibiting a pH-dependent equilibrium between two forms at the virus surface. Membrane fusion is triggered during the transition from the high- to low-pH form. The structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation, in spite of a novel fold combining features of fusion proteins from classes I and II. The structure provides a framework for understanding the reversibility of the G conformational change. Unexpectedly, G is homologous to gB of herpesviruses, which raises important questions on viral evolution.