Cytoplasmic Cargo Receptor p62 Inhibits Avibirnavirus Replication by Mediating Autophagic Degradation of Viral Protein VP2.
Animals
Autophagy
/ drug effects
Avibirnavirus
/ drug effects
Birnaviridae Infections
/ virology
Capsid Proteins
/ metabolism
Chickens
Cytosol
/ metabolism
Gene Knockout Techniques
HEK293 Cells
Humans
RNA-Binding Proteins
/ genetics
Ubiquitin
/ metabolism
Viral Proteins
/ metabolism
Virus Replication
/ drug effects
VP2
autophagy
avibirnavirus
cargo receptor
p62
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
23 11 2020
23 11 2020
Historique:
received:
22
06
2020
accepted:
05
09
2020
pubmed:
25
9
2020
medline:
26
1
2021
entrez:
24
9
2020
Statut:
epublish
Résumé
Selective autophagy regulates the degradation of cytoplasmic cargos, such as damaged organelles, invading pathogens, and aggregated proteins. Furthermore, autophagy is capable of degrading avibirnavirus, but the mechanism responsible for this process is unclear. Here, we show that autophagy cargo receptor p62 regulates the degradation of the avibirnavirus capsid protein VP2. Binding of p62 to VP2 enhances autophagic induction and promotes autophagic degradation of viral protein VP2. Further study showed that the interaction of p62 with viral protein VP2 is dependent on ubiquitination at the K411 site of VP2 and the ubiquitin-associated domain of p62. Mutation analysis showed that the K411R mutation of viral protein VP2 prohibits its p62-mediated degradation. Consistent with this finding, p62 lacking the ubiquitin-associated domain or the LC3-interacting region no longer promoted the degradation of VP2. Virus production revealed that the knockout of p62 but not the overexpression of p62 promotes the replication of avibirnavirus. Collectively, our findings suggest that p62 mediates selective autophagic degradation of avibirnavirus protein VP2 in a ubiquitin-dependent manner and is an inhibitor of avibirnavirus replication.
Identifiants
pubmed: 32967959
pii: JVI.01255-20
doi: 10.1128/JVI.01255-20
pmc: PMC7925189
pii:
doi:
Substances chimiques
Capsid Proteins
0
P62 protein, human
0
RNA-Binding Proteins
0
Ubiquitin
0
Viral Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2020 Li et al.
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