Institute of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
Institute of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu 212013, China; School of Public Health, University of California, Berkeley, CA, USA.
Life Sci. 2018 Aug 15;207:350-354. doi: 10.1016/j.lfs.2018.06.014. Epub 2018 Jun 18.
Protein ubiquitination is a highly conserved post-translational modification affecting various biological processes including viral propagation. Ubiquitination has multiple effects on viral propagation, including viral genome uncoating, viral replication, and immune evasion. Ubiquitination of viral proteins is triggered by the ubiquitin-proteasome system (UPS). This involves the covalent attachment of the highly conserved 76 amino acid residue ubiquitin protein to target proteins by the consecutive actions of E1, E2 and E3 enzymes, and the 26S proteasome that together form a multiprotein complex that degrades target proteins. The UPS is the primary cytosolic proteolytic machinery for the selective degradation of various forms of proteins including viral proteins, thereby limiting viral growth in host cells. To combat this host anti-viral machinery, viruses have evolved the ability to employ or subvert the UPS to inactivate or degrade cellular proteins to favour viral propagation. This review highlights our current knowledge on the different roles of the UPS during viral propagation.
蛋白质泛素化是一种高度保守的翻译后修饰,影响多种生物过程,包括病毒的繁殖。泛素化对病毒的繁殖有多种影响,包括病毒基因组脱壳、病毒复制和免疫逃逸。病毒蛋白的泛素化是由泛素-蛋白酶体系统(UPS)触发的。这涉及到通过 E1、E2 和 E3 酶的连续作用,将高度保守的 76 个氨基酸残基的泛素蛋白共价连接到靶蛋白上,以及 26S 蛋白酶体,它们共同形成一个多蛋白复合物,降解靶蛋白。UPS 是细胞质中用于选择性降解各种形式蛋白质(包括病毒蛋白质)的主要蛋白酶体机制,从而限制了宿主细胞中病毒的生长。为了对抗这种宿主抗病毒机制,病毒已经进化出利用或颠覆 UPS 的能力,使细胞蛋白失活或降解,以促进病毒的繁殖。这篇综述强调了我们目前对 UPS 在病毒繁殖过程中不同作用的认识。