Herpesvirus gB: A Finely Tuned Fusion Machine.
Herpesvirus gB: A Finely Tuned Fusion Machine.
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DOI：
10.3390/v7122957
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发表时间：
2015-12-11
期刊：
影响因子：
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通讯作者：
Heldwein EE
中科院分区：
文献类型：
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作者：
Cooper RS;Heldwein EE
包膜病毒利用一类被称为融合原的蛋白质来协调其周围的包膜和目标细胞膜的合并。大多数融合原通过结合细胞受体并随后催化膜融合过程来单独完成这项任务。令人惊讶的是，在疱疹病毒中，这些功能分布在多种蛋白质中：保守的融合原gB，功能不明确的保守gH/gL异二聚体，以及各种非保守的受体结合蛋白。我们总结了目前已知的两种密切相关的疱疹病毒，HSV-1和HSV-2的gB，重点是这种融合原的大部分未知的膜相互作用区域的结构。我们认为这种不寻常的疱疹病毒融合机制可能与gB的独特结构有关。
Enveloped viruses employ a class of proteins known as fusogens to orchestrate the merger of their surrounding envelope and a target cell membrane. Most fusogens accomplish this task alone, by binding cellular receptors and subsequently catalyzing the membrane fusion process. Surprisingly, in herpesviruses, these functions are distributed among multiple proteins: the conserved fusogen gB, the conserved gH/gL heterodimer of poorly defined function, and various non-conserved receptor-binding proteins. We summarize what is currently known about gB from two closely related herpesviruses, HSV-1 and HSV-2, with emphasis on the structure of the largely uncharted membrane interacting regions of this fusogen. We propose that the unusual mechanism of herpesvirus fusion could be linked to the unique architecture of gB.