Well Put Together-A Guide to Accessorizing with the Herpesvirus gH/gL Complexes.
Well Put Together-A Guide to Accessorizing with the Herpesvirus gH/gL Complexes.
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DOI：
10.3390/v14020296
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发表时间：
2022-01-30
期刊：
影响因子：
--
通讯作者：
Heldwein EE
中科院分区：
文献类型：
--
作者：
Gonzalez-Del Pino GL;Heldwein EE
疱疹病毒是一种被包膜的双链DNA病毒，可以感染动物界的各种宿主。其中9种在人类中造成终身感染，目前没有治愈方法，也没有多少疫苗或治疗方案。像所有包膜病毒一样，疱疹病毒通过脂质包膜与宿主细胞膜融合进入细胞。独特的是，疱疹病毒将受体结合和膜融合的功能分布在多种糖蛋白上。两种糖蛋白复合物在三个疱疹病毒亚家族中都是保守的：三聚体gB作为膜融合原和异二聚体gH/gL，其作用不太明确。在这里，我们通过比较gH/gL与广泛的辅助病毒蛋白、宿主细胞受体和中和或抑制抗体的相互作用，强调了gH/gL在人类疱疹病毒三个亚家族中的保守和不同功能。我们认为gH/gL固有的结构可塑性使其能够作为信号集成机器，接受各种调节输入并将其转换为激活gB融合能力的“触发”信号。
Herpesviruses are enveloped, double-stranded DNA viruses that infect a variety of hosts across the animal kingdom. Nine of these establish lifelong infections in humans, for which there are no cures and few vaccine or treatment options. Like all enveloped viruses, herpesviruses enter cells by fusing their lipid envelopes with a host cell membrane. Uniquely, herpesviruses distribute the functions of receptor engagement and membrane fusion across a diverse cast of glycoproteins. Two glycoprotein complexes are conserved throughout the three herpesvirus subfamilies: the trimeric gB that functions as a membrane fusogen and the heterodimeric gH/gL, the role of which is less clearly defined. Here, we highlight the conserved and divergent functions of gH/gL across the three subfamilies of human herpesviruses by comparing its interactions with a broad range of accessory viral proteins, host cell receptors, and neutralizing or inhibitory antibodies. We propose that the intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a “trigger” signal that activates the fusogenic ability of gB.
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