TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation.
Journal
PLoS pathogens
ISSN: 1553-7374
Titre abrégé: PLoS Pathog
Pays: United States
ID NLM: 101238921
Informations de publication
Date de publication:
09 2021
09 2021
Historique:
received:
15
06
2021
accepted:
17
08
2021
revised:
23
09
2021
pubmed:
14
9
2021
medline:
27
11
2021
entrez:
13
9
2021
Statut:
epublish
Résumé
Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3-6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation of antiviral effectors to restrict viral replication. Here, we conducted RNA-seq in avian cells infected by IBDV and identified TRIM25 as a host restriction factor. Specifically, TRIM25 deficiency dramatically increased viral yields, whereas overexpression of TRIM25 significantly inhibited IBDV replication. Immunoprecipitation assays indicated that TRIM25 only interacted with VP3 among all viral proteins, mediating its K27-linked polyubiquitination and subsequent proteasomal degradation. Moreover, the Lys854 residue of VP3 was identified as the key target site for the ubiquitination catalyzed by TRIM25. The ubiquitination site destroyed enhanced the replication ability of IBDV in vitro and in vivo. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3.
Identifiants
pubmed: 34516573
doi: 10.1371/journal.ppat.1009900
pii: PPATHOGENS-D-21-01252
pmc: PMC8459960
doi:
Substances chimiques
Tripartite Motif Proteins
0
VP3 protein, infectious bursal disease virus
0
Viral Structural Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1009900Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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