Porcine Picornavirus 3C Protease Degrades PRDX6 to Impair PRDX6-mediated Antiviral Function.
3Cpro
Antagonism
Peroxiredoxin-6 (PRDX6)
Phospholipase A2 (PLA2)
Porcine picornavirus
Journal
Virologica Sinica
ISSN: 1995-820X
Titre abrégé: Virol Sin
Pays: Netherlands
ID NLM: 101514185
Informations de publication
Date de publication:
Oct 2021
Oct 2021
Historique:
received:
30
09
2020
accepted:
17
12
2020
pubmed:
16
3
2021
medline:
3
11
2021
entrez:
15
3
2021
Statut:
ppublish
Résumé
Peroxiredoxin-6 (PRDX6) is an antioxidant enzyme with both the activities of peroxidase and phospholipase A2 (PLA2), which is involved in regulation of many cellular reactions. However, the function of PRDX6 during virus infection remains unknown. In this study, we found that the abundance of PRDX6 protein was dramatically decreased in foot-and-mouth disease virus (FMDV) infected cells. Overexpression of PRDX6 inhibited FMDV replication. In contrast, knockdown of PRDX6 expression promoted FMDV replication, suggesting an antiviral role of PRDX6. To explore whether the activity of peroxidase and PLA2 was associated with PRDX6-mediated antiviral function, a specific inhibitor of PLA2 (MJ33) and a specific inhibitor of peroxidase activity (mercaptosuccinate) were used to treat the cells before FMDV infection. The results showed that incubation of MJ33 but not mercaptosuccinate promoted FMDV replication. Meanwhile, overexpression of PRDX6 slightly enhanced type I interferon signaling. We further determined that the viral 3C
Identifiants
pubmed: 33721217
doi: 10.1007/s12250-021-00352-4
pii: 10.1007/s12250-021-00352-4
pmc: PMC7957437
doi:
Substances chimiques
Antiviral Agents
0
Peroxiredoxin VI
EC 1.11.1.15
Peptide Hydrolases
EC 3.4.-
Cysteine Endopeptidases
EC 3.4.22.-
3C Viral Proteases
EC 3.4.22.28
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
948-957Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2021. Wuhan Institute of Virology, CAS.
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