a Laboratory of Intracellular Signaling, Moscow Institute of Physics and Technology , Dolgoprudny, Moscow Region , Russian Federation.
b Laboratory of Molecular Biology and Biochemistry, Institute of Molecular Medicine, Sechenov First Moscow State Medical University , Moscow , Russian Federation.
Cell Cycle. 2019 Sep;18(17):1995-2005. doi: 10.1080/15384101.2019.1639305. Epub 2019 Jul 10.
The process of protein post-translational modifications (PTM) is one of the critical mechanisms of regulation of many cellular processes, which makes it an attractive target for various viruses. Since viruses cannot replicate on their own, they have developed unique abilities to alter metabolic and signaling cell pathways, including protein PTMs, to ensure faithful replication of their genomes. This review describes several ways of how lysine-specific PTMs are used by various viruses to ensure its successful invasion and replication. Covalent modifications like acetylation, ubiquitination, and methylation form a complex system of reversible and often competing modifications, which adds an additional level of complexity to the system of regulation of the activity of host proteins involved in viral replication and propagation. In furthering these, we also describe the manner in which PTM pathways can also be accosted by various types of viruses to neutralize the host's cellular mechanisms for anti-viral protection and highlight key areas for future therapeutic targeting and design.
蛋白质翻译后修饰（PTM）过程是许多细胞过程调节的关键机制之一，这使其成为各种病毒的有吸引力的靶标。由于病毒本身不能复制，它们已经发展出独特的能力来改变代谢和信号细胞途径，包括蛋白质 PTM，以确保其基因组的忠实复制。这篇综述描述了几种赖氨酸特异性 PTM 被各种病毒用来确保其成功入侵和复制的方式。乙酰化、泛素化和甲基化等共价修饰形成了一个复杂的可逆且经常相互竞争的修饰系统，这为参与病毒复制和传播的宿主蛋白活性调节系统增加了一个额外的复杂性。在进一步研究中，我们还描述了各种类型的病毒如何攻击 PTM 途径，以中和宿主的抗病毒保护机制，并强调未来治疗靶向和设计的关键领域。
