Protein kinase Cdc7 supports viral replication by phosphorylating Avibirnavirus VP3 protein.

Autor:	Deng T; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China.; College of Veterinary Medicine, Southwest University , Chongqing, China., Du L; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China., Ding S; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China., Peng X; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China., Chen W; Collaborative Innovation Center and State Key Laboratory for Diagnosis and Treatment of Infectious Diseases, First Affiliated Hospital, Zhejiang University , Hangzhou, China., Yan Y; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China., Hu B; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China., Zhou J; MOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University , Hangzhou, China.; Collaborative Innovation Center and State Key Laboratory for Diagnosis and Treatment of Infectious Diseases, First Affiliated Hospital, Zhejiang University , Hangzhou, China.
Jazyk:	angličtina
Zdroj:	Journal of virology [J Virol] 2023 Nov 30; Vol. 97 (11), pp. e0112523. Date of Electronic Publication: 2023 Oct 30.
DOI:	10.1128/jvi.01125-23
Abstrakt:	Importance: The Avibirnavirus infectious bursal disease virus is still an important agent which largely threatens global poultry farming industry economics. VP3 is a multifunctional scaffold structural protein that is involved in virus morphogenesis and the regulation of diverse cellular signaling pathways. However, little is known about the roles of VP3 phosphorylation during the IBDV life cycle. In this study, we determined that IBDV infection induced the upregulation of Cdc7 expression and phosphorylated the VP3 Ser13 site to promote viral replication. Moreover, we confirmed that the negative charge addition of phosphoserine on VP3 at the S13 site was essential for IBDV proliferation. This study provides novel insight into the molecular mechanisms of VP3 phosphorylation-mediated regulation of IBDV replication. Competing Interests: The authors declare no conflict of interest.
Databáze:	MEDLINE
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