PRRSV NSP1α degrades TRIM25 through proteasome system to inhibit host antiviral immune response

文献类型： 外文期刊

第一作者： Zheng, Yuhang

作者： Zheng, Yuhang;Wang, Zhao;Du, Yijun;Qi, Jing;Huang, Juan;Lu, Yu;Lu, Yu;Jiang, Dandan;Wu, Xiangju;Hu, Yue;Cong, Xiaoyan;Li, Juntong;Du, Yijun;Qi, Jing;Sui, Chao;Wang, Zhao;Wang, Zhao;Lee, Changhee

作者机构：

关键词： PRRSV NSP1 alpha; TRIM25; Proteasome system; Antiviral response

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：2.4； 五年影响因子：2.6 ）

ISSN： 0378-1135

年卷期： 2024 年 296 卷

页码：

收录情况： SCI

摘要： Porcine reproductive and respiratory syndrome (PRRS) is the most economically significant disease caused by porcine reproductive and respiratory syndrome virus (PRRSV). Type I interferon (IFN) induces a large number of interferon-stimulated genes (ISGs) expression to inhibit PRRSV infection. To survive in the host, PRRSV has evolved multiple strategies to antagonize host innate immune response. Previous studies have reported that PRRSV N protein decreases the expression of TRIM25 and TRIM25-mediated RIG-I ubiquitination to suppress IFN-beta production. However, whether other PRRSV proteins inhibit the antiviral function of TRIM25 is less well understood. In this study, we first found that PRRSV NSP1 alpha decreased ISGylation of TRIM25. Meanwhile, NSP1 alpha significantly suppressed TRIM25-mediated IFN-beta production to promote PRRSV replication. Further studies demonstrated that PRRSV NSP1 alpha reduced the protein level of TRIM25 in proteasome system but did not regulate the transcription level of TRIM25. In addition, the function of NSP1 alpha in TRIM25 degradation did not rely on its papain-like cysteine protease activity. Taken together, PRRSV NSP1 alpha antagonizes the antiviral response of TRIM25 by mediating TRIM25 degradation to promote PRRSV replication. Our data identify TRIM25 as a natural target of PRRSV NSP1 alpha and reveal a novel mechanism that PRRSV induces TRIM25 degradation and inhibits host antiviral immune response.

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