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），在许多细胞过程（包括表观遗传学，肿瘤抑制，肿瘤发生，DNA损伤反应，免疫力和病毒感染）的调节中起关键作用。USP7是第一个与病毒感染相关的DUB。从那以后，发现了其他DUB：病毒蛋白相互作用，但是，USP7仍然是与各种病毒的许多蛋白相互作用的最有针对性的DUB。进化的选择性压力使病毒能够发展破坏宿主细胞机制的机制，从而促进病毒生态位的存活。已经鉴定出许多病毒蛋白可以靶向和篡改USP7的功能以发挥其优势。