Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry
Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry
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DOI：
10.1016/j.coviro.2012.10.005
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发表时间：
2013-02-01
影响因子：
5.9
通讯作者：
Heldwein, Ekaterina E.
中科院分区：
文献类型：
--
作者：
Stampfer, Samuel D.;Heldwein, Ekaterina E.
包膜病毒通过融合病毒和细胞膜进入细胞，并且大多数使用结合受体结合和融合功能的单个病毒包膜蛋白。在疱疹病毒中，这些功能分布在多个蛋白质中：保守的融合蛋白gB，各种非保守的受体结合蛋白，以及保守的gH/gL异源二聚体，奇怪的是，在其他包膜病毒中缺乏明显的对应物。最近对HSV-2和EBV的gH/gL的结构研究揭示了一种独特的复合物，与其他病毒蛋白没有结构或功能相似性。在这里，我们分析了gH/gL结构，并强调了重要的功能区域。我们建议，gH/gL的功能作为一个适配器，传输触发信号从各种非保守的输入高度保守的融合蛋白gB。
Enveloped viruses enter cells by fusing the viral and cellular membranes, and most use a single viral envelope protein that combines receptor-binding and fusogenic functions. In herpesviruses, these functions are distributed among multiple proteins: the conserved fusion protein gB, various non-conserved receptor-binding proteins, and the conserved gH/gL heterodimer that curiously lacks an apparent counterpart in other enveloped viruses. Recent structural studies of gH/gL from HSV-2 and EBV revealed a unique complex with no structural or functional similarity to other viral proteins. Here we analyzed gH/gL structures and highlighted important functional regions. We propose that gH/gL functions as an adaptor that transmits the triggering signals from various non-conserved inputs to the highly conserved fusion protein gB.