Department of Biology, York University, Toronto, Canada.
Department of Biology, York University, Toronto, Canada.
Virus Res. 2020 Sep;286:198076. doi: 10.1016/j.virusres.2020.198076. Epub 2020 Jun 27.
Ubiquitin Specific Protease 7 (USP7) is a deubiquitinating enzyme (DUB) that plays critical roles in the regulation of many cellular processes including epigenetics, tumour suppression, oncogenesis, DNA damage response, immunity and viral infection. USP7 was the first DUB associated with viral infection. Since then other DUB:viral protein interactions have been discovered, however, USP7 continues to be the most targeted DUB interacting with many proteins from various viruses. The selective pressures of evolution have allowed viruses to develop mechanisms that subvert host cellular machinery, promoting survival of the viral niche. Numerous viral proteins have been identified to target and usurp the function of USP7 to their advantage. This review explores novel developments in research focusing on the mechanisms underlying the manipulation of USP7 by viruses.
泛素特异性蛋白酶 7（USP7）是一种去泛素化酶（DUB），在调节许多细胞过程中发挥关键作用，包括表观遗传学、肿瘤抑制、致癌作用、DNA 损伤反应、免疫和病毒感染。USP7 是第一个与病毒感染相关的 DUB。此后，发现了其他 DUB：病毒蛋白相互作用，但 USP7 仍然是与来自各种病毒的许多蛋白质相互作用的最受靶向的 DUB。进化的选择压力使病毒能够开发出颠覆宿主细胞机制的机制，促进病毒小生境的存活。已经鉴定出许多病毒蛋白作为靶点，并篡夺 USP7 的功能以获得优势。这篇综述探讨了研究的新进展，重点是病毒操纵 USP7 的机制。
