Enterovirus 71 3C proteolytically processes the histone H3 N-terminal tail during infection

Virol Sin. 2022 Apr;37(2):314-317. doi: 10.1016/j.virs.2022.02.006. Epub 2022 Feb 18.

¹ Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, 430072, China; Institute of Biochemistry, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, 310018, China. Electronic address: miaom@whu.edu.cn.
² Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
³ Laboratory of RNA Virology, Wuhan Institute of Virology, Chinese Academy of Science, Wuhan, 430071, China.
⁴ Institute of Biochemistry, College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
⁵ Laboratory of RNA Virology, Wuhan Institute of Virology, Chinese Academy of Science, Wuhan, 430071, China. Electronic address: zhouxi@whu.edu.cn.
⁶ Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, 430072, China. Electronic address: zhaoxiaolu@whu.edu.cn.

Abstract

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The N-terminal tail of histone H3 is specifically cleaved during EV71 infection.
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Viral protease 3C is identified as a protease responsible for proteolytically processing the N-terminal H3 tail.
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Our finding reveals a new epigenetic regulatory mechanism for Enterovirus 71 in virus-host interactions.