Nucleocapsid protein of porcine reproductive and respiratory syndrome virus antagonizes the antiviral activity of TRIM25 by interfering with TRIM25-mediated RIG-I ubiquitination

文献类型： 外文期刊

第一作者： Zhao, Kuan

作者： Zhao, Kuan;Li, Li-Wei;Jiang, Yi-Feng;Gao, Fei;Zhang, Yu-Jiao;Zhao, Wen-Ying;Li, Guo-Xin;Yu, Ling-Xue;Zhou, Yan-Jun;Tong, Guang-Zhi;Li, Li-Wei;Jiang, Yi-Feng;Gao, Fei;Li, Guo-Xin;Yu, Ling-Xue;Zhou, Yan-Jun;Tong, Guang-Zhi

作者机构：

关键词： TRIM25; PRRSV; N Protein; RIG-I; Ubiquitination

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.293； 五年影响因子：3.599 ）

ISSN： 0378-1135

年卷期： 2019 年 233 卷

页码：

收录情况： SCI

摘要： Porcine reproductive and respiratory syndrome (PRRS) is caused by PRRS virus (PRRSV), and is characterized be respiratory diseases in piglet and reproductive disorders in sow. Identification of sustainable and effective measures to mitigate PRRSV transmission is a pressing problem. The nucleocapsid (N) protein of PRRSV plays crucial role in inhibiting host innate immunity during PRRSV infection. In the current study, a new host-re stricted factor, tripartite motif protein 25 (TRIM25), was identified as an inhibitor of PRRSV replication. Cc immunoprecipitation assay indicated that the PRRSV N protein interferes with TRIM25 RIG-I interactions by competitively interacting with TRIM25. Furthermore, N protein inhibits the expression of TRIM25 and TRIM25 mediated RIG-I ubiquitination to suppress interferon 13 production. Furthermore, with increasing TRIM25 ex pression, the inhibitory effect of N protein on the ubiquitination of RIG-I diminished. These results indicate for the first time that TRIM25 inhibits PRRSV replication and that the N protein antagonizes the antiviral activity by interfering with TRIM25-mediated RIG-I ubiquitination. This not only provides a theoretical basis for the de velopment of drugs to control PRRSV replication, but also better explains the mechanism through which the PRRSV N protein inhibits innate immune responses of the host.

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