Rey Félix A
Unité de Virologie Structurale and Centre National de la Recherche Scientifique, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France.
EMBO Rep. 2006 Oct;7(10):1000-5. doi: 10.1038/sj.embor.7400807.
This review analyses recent structural results that provide clues about a possible molecular mechanism for the transmission of a fusogenic signal among the envelope glycoproteins of the herpes simplex virus on receptor binding by glycoprotein gD. This signal triggers the membrane-fusion machinery of the virus--contained in glycoproteins gB, gH and gL--to induce the merging of viral and cellular membranes, and to allow virus entry into target cells. This activating process parallels that of gamma-retroviruses, in which receptor binding by the amino-terminal domain of the envelope protein activates the fusogenic potential of the virion in a similar way, despite the different organization of the envelope complexes of these two types of viruses. Therefore, the new structural results on the interaction of gD with its receptors might also provide insights into the mechanism of fusogenic signal transmission in gamma-retroviruses. Furthermore, the fusion activation parallels with retroviruses, together with the recently reported structural homology of gB with the rhabdovirus envelope glycoprotein indicate that the complex entry apparatus of herpesviruses appears to be functionally related to that of simpler enveloped viruses.
本综述分析了近期的结构研究结果，这些结果为单纯疱疹病毒包膜糖蛋白在糖蛋白gD与受体结合时传递融合信号的可能分子机制提供了线索。该信号触发病毒的膜融合机制（包含在糖蛋白gB、gH和gL中），诱导病毒膜与细胞膜融合，使病毒进入靶细胞。这一激活过程与γ逆转录病毒的激活过程相似，在γ逆转录病毒中，包膜蛋白的氨基末端结构域与受体结合以类似方式激活病毒粒子的融合潜能，尽管这两类病毒的包膜复合物结构不同。因此，关于gD与其受体相互作用的新结构研究结果也可能为γ逆转录病毒中融合信号传递机制提供见解。此外，与逆转录病毒的融合激活相似，以及最近报道的gB与弹状病毒包膜糖蛋白的结构同源性表明，疱疹病毒复杂的进入机制似乎在功能上与更简单的包膜病毒相关。
