Host E3 ligase Hrd1 ubiquitinates and degrades H protein of canine distemper virus to inhibit viral replication

文献类型： 外文期刊

第一作者： Wang, Wenjie

作者： Wang, Wenjie;Bi, Zhenwei;Wang, Wenjie;Bi, Zhenwei;Song, Suquan;Bi, Zhenwei

作者机构：

关键词： Canine distemper virus; Hrd1; H protein; ubiquitination; replication

期刊名称：VETERINARY RESEARCH （ 影响因子：4.4； 五年影响因子：4.3 ）

ISSN： 0928-4249

年卷期： 2023 年 54 卷 1 期

页码：

收录情况： SCI

摘要： Canine distemper (CD) is a highly contagious and an acutely febrile disease caused by canine distemper virus (CDV), which greatly threatens the dog and fur industry in many countries. Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protein quality control system for the degradation of misfolded proteins in the ER. In this study, a proteomic approach was performed, and results found the E3 ubiquitin ligase 3-hydroxy-3-methylglutaryl reductase degradation protein 1 (Hrd1), which is involved in ERAD, as one of the CDV H-interacting proteins. The interaction of Hrd1 with CDV H protein was further identified by Co-IP assay and confocal microscopy. Hrd1 degraded the CDV H protein via the proteasome pathway dependent on its E3 ubiquitin ligase activity. Hrd1 catalyzed the K63-linked polyubiquitination of CDV H protein at lysine residue 115 (K115). Hrd1 also exhibited a significant inhibitory effect on CDV replication. Together, the data demonstrate that the E3 ligase Hrd1 mediates the ubiquitination of CDV H protein for degradation via the proteasome pathway and inhibits CDV replication. Thus, targeting Hrd1 may represent a novel prevention and control strategy for CDV infection.

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