Herpes simplex virus 1 (HSV-1) hijacks ubiquitination machinery to modify the cellular proteome to create an environment permissive for virus replication. HSV-1 encodes its own RING-finger E3 ubiquitin (Ub) ligase, Infected Cell Protein 0 (ICP0), that directly interfaces with component proteins of the Ub pathway to inactivate host immune defences and cellular processes that restrict the progression of HSV-1 infection. Consequently, ICP0 plays a critical role in the infectious cycle of HSV-1 that is required to promote the efficient onset of lytic infection and productive reactivation of viral genomes from latency. This review will describe the current knowledge regarding the biochemical properties and known substrates of ICP0 during HSV-1 infection. We will highlight the gaps in the characterization of ICP0 function and propose future areas of research required to understand fully the biological properties of this important HSV-1 regulatory protein.

中文翻译：

---

HSV-1 泛素连接酶 ICP0：修改细胞蛋白质组以促进感染。

单纯疱疹病毒 1 (HSV-1) 劫持泛素化机制来修改细胞蛋白质组，以创造一个允许病毒复制的环境。HSV-1 编码其自己的环指 E3 泛素 (Ub) 连接酶，感染细胞蛋白 0 (ICP0)，它直接与 Ub 通路的组成蛋白结合，以灭活宿主免疫防御和限制 HSV-1 进展的细胞过程感染。因此，ICP0 在 HSV-1 的感染周期中起着至关重要的作用，这是促进裂解感染的有效发生和病毒基因组从潜伏期重新激活所必需的。本综述将描述关于 HSV-1 感染期间 ICP0 的生化特性和已知底物的当前知识。