2. Academic Validation
  3. Host E3 ligase Hrd1 ubiquitinates and degrades H protein of canine distemper virus to inhibit viral replication

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

  • Vet Res. 2023 Apr 2;54(1):30. doi: 10.1186/s13567-023-01163-z.
Wenjie Wang 1 2,  Zhenwei Bi 3 4 5,  Suquan Song 2
Affiliations

Affiliations

  • 1 Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture and Rural Affairs, National Center for Engineering Research of Veterinary Bio-Products, Nanjing, 210014, Jiangsu, China.
  • 2 MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, Jiangsu, China.
  • 3 Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture and Rural Affairs, National Center for Engineering Research of Veterinary Bio-Products, Nanjing, 210014, Jiangsu, China. bizhenwei@126.com.
  • 4 MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, Jiangsu, China. bizhenwei@126.com.
  • 5 GuoTai (Taizhou) Center of Technology Innovation for Veterinary Biologicals, Taizhou, 225300, Jiangsu, China. bizhenwei@126.com.
PMID: 37009870 DOI: 10.1186/s13567-023-01163-z
Abstract

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.

Keywords

Canine distemper virus; H protein; Hrd1; replication; ubiquitination.

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