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TRIM21 inhibits porcine epidemic diarrhea virus proliferation by proteasomal degradation of the nucleocapsid protein.

Authors :
Wang, Hua
Chen, Xiaoyong
Kong, Ning
Jiao, Yajuan
Sun, Dage
Dong, Sujie
Qin, Wenzhen
Zhai, Huanjie
Yu, Lingxue
Zheng, Hao
Tong, Wu
Yu, Hai
Tong, Guangzhi
Shan, Tongling
Source :
Archives of Virology; Jul2021, Vol. 166 Issue 7, p1903-1911, 9p
Publication Year :
2021

Abstract

Tripartite motif protein 21 (TRIM21) is an E3 ubiquitin ligase and cytosolic antibody receptor of the TRIM family. Previous reports have indicated that TRIM21 plays an important role during viral infection. This study aimed at examining the role of TRIM21 in the replication of porcine epidemic diarrhea virus (PEDV) and showed that TRIM21 inhibits PEDV proliferation by targeting and degrading the nucleocapsid (N) protein through the proteasomal pathway. Furthermore, the endogenous expression of TRIM21 was found to be downregulated by PEDV infection in Vero and LLC-PK1 cells. Overexpression of TRIM21 inhibited PEDV replication, whereas knockdown of TRIM21 increased viral titers and N protein levels. TRIM21 was found to interact and colocalize with the N protein, and the TRIM21-mediated antiviral effect was dependent on its ubiquitin ligase activity, which engages in polyubiquitination and degradation of the N protein in a proteasome-dependent manner. Taken together, these findings provide information about the role of TRIM21 in PEDV proliferation and increase our understanding of host-virus interactions. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03048608
Volume :
166
Issue :
7
Database :
Complementary Index
Journal :
Archives of Virology
Publication Type :
Academic Journal
Accession number :
150854635
Full Text :
https://doi.org/10.1007/s00705-021-05080-4