Abstract
The ubiquitin (Ub) proteasome system (UPS) plays a pivotal role in regulation of numerous cellular processes, including innate and adaptive immune responses that are essential for restriction of the virus life cycle in the infected cells. Deubiquitination by the deubiquitinating enzyme, deubiquitinase (DUB), is a reversible molecular process to remove Ub or Ub chains from the target proteins. Deubiquitination is an integral strategy within the UPS in regulating survival and proliferation of the infecting virus and the virus-invaded cells. Many viruses in the infected cells are reported to encode viral DUB, and these vial DUBs actively disrupt cellular Ub-dependent processes to suppress host antiviral immune response, enhancing virus replication and thus proliferation. This review surveys the types of DUBs encoded by different viruses and their molecular processes for how the infecting viruses take advantage of the DUB system to evade the host immune response and expedite their replication.
Highlights
It was later demonstrated that SARS-CoV-1 PLpro decreased ubiquitinated forms of RIG-1, stimulator of interferon genes (STING), TRAF3, TANK binding kinase 1 (TBK1), and interleukin regulatory factor 3 (IRF3) to inhibit type I IFN signaling via the STING-TRAF3-TBK1 complex [60]
These results indicate that coronavirus papain-like protease domain 2 (PLP2) comprises multifunctional domains, a viral protease, DUB, and IFN antagonist, suggesting that each domain can serve as an independent target for antiviral therapeutics
Ubiquitination is the process of attaching Ub to target proteins for proteasomal degradation, while deubiquitination antagonizes this process utilizing DUBs to cleave the peptide or isopeptide bond between Ub and its substrate proteins as well as between Ub molecules in a chain
Summary
Post-translational modifications of proteins by ubiquitin (Ub) and Ub-like modifiers (Ubl), such as Nedd, interferon-stimulated gene 15 (ISG15), and small Ub-like modifier (SUMO), have emerged as major regulatory mechanisms in various aspects of cellular activities, including signal transduction, transcription, membrane protein trafficking, autophagy, nuclear transport, and immune responses [1,2,3,4,5]. Eukaryotic viruses take advantage of post-translational modifications for degradation of various viral and cellular proteins to overcome host defense mechanisms at differ of 17 ent stages of the infection cycle. In these processes, both DNA and RNA viruses employ the cellular UPS for degradation [16,17,18,19], while many viruses express their own E3s additional domains, such asproteins, Ub-specific domain, Ubl domain, meprin and class tumorI for degradation of cellular suchproteases as p53, major histocompatibility complex necrosis factor (TNF) receptor factors (TRAF).
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