PTBP1 suppresses porcine epidemic diarrhea virus replication via inducing protein degradation and IFN production

文献类型： 外文期刊

第一作者： Qin, Wenzhen

作者： Qin, Wenzhen;Kong, Ning;Wang, Chunmei;Dong, Sujie;Zhai, Huanjie;Zhai, Xueying;Yang, Xinyu;Ye, Chenqian;Ye, Manqing;Tong, Wu;Liu, Changlong;Yu, Lingxue;Zheng, Hao;Yu, Hai;Tong, Guangzhi;Shan, Tongling;Qin, Wenzhen;Kong, Ning;Tong, Wu;Liu, Changlong;Yu, Lingxue;Zheng, Hao;Yu, Hai;Tong, Guangzhi;Shan, Tongling;Qin, Wenzhen;Lan, Daoliang;Zhang, Yu;Zhang, Wen

作者机构：

期刊名称：JOURNAL OF BIOLOGICAL CHEMISTRY （ 影响因子：4.8； 五年影响因子：4.8 ）

ISSN：

年卷期： 2023 年 299 卷 8 期

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收录情况： SCI

摘要： Porcine epidemic diarrhea virus (PEDV) causes severe morbidity and mortality among newborn piglets. It significantly threatens the porcine industry in China and around the globe. To accelerate the developmental pace of drugs or vaccines against PEDV, a deeper understanding of the interaction between viral proteins and host factors is crucial. The RNAbinding protein, polypyrimidine tract-binding protein 1 (PTBP1), is crucial for controlling RNA metabolism and biological processes. The present work focused on exploring the effect of PTBP1 on PEDV replication. PTBP1 was upregulated during PEDV infection. The PEDV nucleocapsid (N) protein was degraded through the autophagic and proteasomal degradation pathways. Moreover, PTBP1 recruits MARCH8 (an E3 ubiquitin ligase) and NDP52 (a cargo receptor) for N protein catalysis and degradation through selective autophagy. Furthermore, PTBP1 induces the host innate antiviral response via upregulating the expression of MyD88, which then regulates TNF receptor- associated factor 3/ TNF receptor-associated factor 6 expression and induces the phosphorylation of TBK1 and IFN regulatory factor 3. These processes activate the type I IFN signaling pathway to antagonize PEDV replication. Collectively, this work illustrates a new mechanism related to PTBP1-induced viral restriction, where PTBP1 degrades the viral N protein and induces type I IFN production to suppress PEDV replication.

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