Deubiquitylating enzymes (DUBs) are proteases that crack the ubiquitin code from ubiquitylated substrates to reverse the fate of substrate proteins. Recently, DUBs have been found to mediate various cellular biological functions, including antiviral innate immune response mediated by pattern-recognition receptors (PRRs) and NLR Family pyrin domain containing 3 (NLRP3) inflammasomes. So far, many DUBs have been identified to exert a distinct function in fine-tuning antiviral innate immunity and are utilized by viruses for immune evasion. Here, the recent advances in the regulation of antiviral responses by DUBs are reviewed. We also discussed the DUBs-mediated interaction between the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and antiviral innate immunity. The understanding of the mechanisms on antiviral innate immunity regulated by DUBs may provide therapeutic opportunities for viral infection.
【저자키워드】 SARS-CoV-2, Innate immunity, virus, immune evasion, Inflammasome, deubiquitylating enzymes, pattern-recognition receptors, 【초록키워드】 Biological functions, viral infection, coronavirus, innate immune response, Antiviral, Proteins, protease, virus, family, therapeutic, receptor, mechanism, NLRP3, NLR, cellular, antiviral response, Interaction, inflammasomes, acute respiratory syndrome, Regulation, PRRs, enzyme, domain, substrate, regulated, DUB, 【제목키워드】 Innate, Factor,