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Porcine Reproductive and Respiratory Syndrome Virus Antagonizes JAK/STAT3 Signaling via nsp5, Which Induces STAT3 Degradation

文献类型： 外文期刊

作者： Yang, Liping 1 ; Wang, Rong 2 ; Ma, Zexu 1 ; Xiao, Yueqiang 3 ; Nan, Yuchen 4 ; Wang, Yu 5 ; Lin, Shaoli 1 ; Zhang, Yan-J 1 ;

作者机构： 1.Univ Maryland, VA MD Coll Vet Med, Mol Virol Lab, College Pk, MD 20742 USA; Univ Maryland, Maryland Pathogen Res Inst, College Pk, MD 20742 USA

2.Xi An Jiao Tong Univ, Sch Med, Lab Anim Ctr, Xian, Shaanxi, Peoples R China

3.Shandong Acad Agr Sci, Shandong Binzhou Anim Sci & Vet Med Acad, Binzhou Branch, Binzhou, Shandong, Peoples R China

4.Northwest A&F Univ, Coll Vet Med, Dept Vet Prevent Med, Yangling, Shaanxi, Peoples R China

5.Taishan Med Univ, Coll Basic Med Sci, Tai An, Shandong, Peoples R China

关键词： porcine reproductive and respiratory syndrome virus (PRRSV);signal transducer and activator of transcription 3;STAT3;JAK/STAT signaling;innate immunity;PRRSV nsp5

期刊名称：JOURNAL OF VIROLOGY （ 影响因子：5.103； 五年影响因子：5.078 ）

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收录情况： SCI

摘要： Signal transducer and activator of transcription 3 (STAT3) is a pleiotropic signaling mediator of many cytokines, including interleukin-6 (IL-6) and IL-10. STAT3 is known to play critical roles in cell growth, proliferation, differentiation, immunity and inflammatory responses. The objective of this study was to determine the effect of porcine reproductive and respiratory syndrome virus (PRRSV) infection on the STAT3 signaling since PRRSV induces a weak protective immune response in host animals. We report here that PRRSV infection of MARC-145 cells and primary porcine pulmonary alveolar macrophages led to significant reduction of STAT3 protein level. Several strains of both PRRSV type 1 and type 2 led to a similar reduction of STAT3 protein level but had a minimal effect on its transcripts. The PRRSV-mediated STAT3 reduction was in a dose-dependent manner as the STAT3 level decreased, along with incremental amounts of PRRSV inocula. Further study showed that nonstructural protein 5 (nsp5) of PRRSV induced the STAT3 degradation by increasing its polyubiquitination level and shortening its half-life from 24 h to similar to 3.5 h. The C-terminal domain of nsp5 was shown to be required for the STAT3 degradation. Moreover, the STAT3 signaling in the cells transfected with nsp5 plasmid was significantly inhibited. These results indicate that PRRSV antagonizes the STAT3 signaling by accelerating STAT3 degradation via the ubiquitin-proteasomal pathway. This study provides insight into the PRRSV interference with the JAK/STAT3 signaling, leading to perturbation of the host innate and adaptive immune responses.

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