PRRSV NSP1α degrades TRIM25 through proteasome system to inhibit host antiviral immune response
文献类型： 外文期刊
作者： Zheng, Yuhang 1 ; Jiang, Dandan 4 ; Sui, Chao 5 ; Wu, Xiangju 4 ; Hu, Yue 4 ; Lee, Changhee 8 ; Cong, Xiaoyan 4 ; Li, Juntong 4 ; Lu, Yu 2 ; Wang, Zhao 1 ; Du, Yijun 1 ; Qi, Jing 1 ; Huang, Juan 1 ;
作者机构： 1.Qingdao Agr Univ, Coll Vet Med, Qingdao 266109, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Vet Immunol & Engn, Nanjing 210014, Peoples R China
3.GuoTai Taizhou Ctr Technol Innovat Vet Biol, Nanjing 210014, Peoples R China
4.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Key Lab Livestock & Poultry Multi MARA, Jinan 250100, Peoples R China
5.Shandong Univ, Qilu Hosp, Lab Anim Ctr, Jinan 250012, Peoples R China
6.Shandong First Med Univ & Shandong Acad Med Sci, Sch Lab Anim, Jinan, Peoples R China
7.Shandong First Med Univ & Shandong Acad Med Sci, Shandong Lab Anim Ctr, Jinan 250118, Peoples R China
8.Gyeongsang Natl Univ, Coll Vet Med, Virus Vaccine Res Ctr, Jinju 52828, South Korea
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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