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Biochem Biophys Res Commun. 2019 Nov 4. pii: S0006-291X(19)32057-1. doi: 10.1016/j.bbrc.2019.10.147. [Epub ahead of print]

Ebola virus replication is regulated by the phosphorylation of viral protein VP35.

Author information

1
College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, PR China; Beijing Institute of Biotechnology, 27 Taiping Rd, Haidian District, Beijing, 100850, PR China.
2
Beijing Institute of Biotechnology, 27 Taiping Rd, Haidian District, Beijing, 100850, PR China.
3
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, PR China.
4
Institut Pasteur of Shanghai, Chinese Academy of Sciences, 200031, Shanghai, PR China.
5
National Engineering Research Center for the Emergency Drug, Beijing Institute of Pharmacology and Toxicology, Beijing, 100850, PR China.
6
College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, PR China; Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun, 130000, PR China. Electronic address: xiaxzh@cae.cn.
7
Beijing Institute of Biotechnology, 27 Taiping Rd, Haidian District, Beijing, 100850, PR China. Electronic address: cao_c@sohu.com.

Abstract

Ebola virus (EBOV) is a zoonotic pathogen, the infection often results in severe, potentially fatal, systematic disease in human and nonhuman primates. VP35, an essential viral RNA-dependent RNA polymerase cofactor, is indispensable for Ebola viral replication and host innate immune escape. In this study, VP35 was demonstrated to be phosphorylated at Serine/Threonine by immunoblotting, and the major phosphorylation sites was S187, S205, T206, S208 and S317 as revealed by LC-MS/MS. By an EBOV minigenomic system, EBOV minigenome replication was shown to be significantly inhibited by the phosphorylation-defective mutant, VP35 S187A, but was potentiated by the phosphorylation mimic mutant VP35 S187D. Together, our findings demonstrate that EBOV VP35 is phosphorylated on multiple residues in host cells, especially on S187, which may contribute to efficient viral genomic replication and viral proliferation.

KEYWORDS:

EBOV replication; Minigenome; Phosphorylation; S187; VP35

PMID:
31694758
DOI:
10.1016/j.bbrc.2019.10.147

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