泛素化修饰在细胞生理过程维持中起着至关重要的作用，而去泛素化酶(deubiquitinating enzymes, DUBs)通过特异性移除靶蛋白上的泛素分子，以维持细胞内泛素化修饰的动态平衡。泛素特异性蛋白酶(ubiquitin specific protease, USP)作为DUBs家族中的重要组成，因其高度的多样性和特异性，在调控病毒复制和宿主免疫应答中发挥着关键作用。研究表明，不同USP蛋白依赖迥然不同的分子策略，可以正向或负向调控病毒复制，影响宿主的抗病毒免疫反应。其中，USP4、USP8、USP13、USP15和USP49等成员在抗病毒免疫中具有积极作用，而USP1、USP7、USP33和UL36泛素特异性蛋白酶(UL36USP)等则可能抑制宿主的免疫反应。本文综述了USP家族成员在抗病毒免疫应答中的调控机制，并探讨了这些调控机制的最新研究进展。这些研究不仅揭示了USPs在病毒与宿主相互作用中的复杂角色，而且为开发针对病毒的新型治疗策略提供了潜在的分子作用靶标和理论依据。

Ubiquitination plays an important role in many biological processes, including viral infections, and can be reversed by deubiquitinating enzymes (DUBs). Although some studies have found that DUBs can either inhibit or enhance viral infection through various mechanisms, the role of DUBs in viral regulation is still unknown and needs to be further explored. Ubiquitin specific protease (USP) belongs to cysteine protease and is one of the important members of deubiquitination enzyme family. USP family members affect viral replication through positive or negative regulatory mechanisms in a variety of ways. For example, USP4, USP8, USP13, USP15 and USP49 have antiviral effects, while USP1, USP7, USP33 and UL36USP negatively regulate the antiviral immune response of the body. This review aims to comprehensively summarize the regulatory mechanisms and research progress of USP family members in antiviral immune response, which not only reveals the complex role of these proteases in virus-host interactions, but also provides valuable molecular targets and theoretical basis for the development of novel antiviral strategies. With the deepening of research, the multifaceted nature of USPs in virus infection and prevention and control will gradually become clear, offering new solutions to global public health challenges.