Cryo-EM structure of the varicella-zoster virus A-capsid

Junqing Sun, Congcong Liu, Ruchao Peng, Fu-Kun Zhang, Zhou Tong, Sheng Liu, Yi Shi, Zhennan Zhao, Wen-Bo Zeng, George Fu Gao, Hong-Jie Shen, Xiaoming Yang (), Minhua Luo (), Jianxun Qi () and Peiyi Wang ()
Additional contact information
Junqing Sun: Shanxi Academy of Advanced Research and Innovation
Congcong Liu: Southern University of Science and Technology
Ruchao Peng: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS)
Fu-Kun Zhang: Changchun Keygen Biological Products Co. Ltd.
Zhou Tong: Shanxi Academy of Advanced Research and Innovation
Sheng Liu: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS)
Yi Shi: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS)
Zhennan Zhao: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS)
Wen-Bo Zeng: State Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology, Center for Biosafety Mega-Science, Wuhan Institute of Virology, Chinese Academy of Sciences
George Fu Gao: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS)
Hong-Jie Shen: Changchun Keygen Biological Products Co. Ltd.
Xiaoming Yang: China National Pharmaceutical Group Corporation
Minhua Luo: University of Chinese Academy of Sciences
Jianxun Qi: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS)
Peiyi Wang: Southern University of Science and Technology

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily, causes severe diseases in humans of all ages. The viral capsids play critical roles in herpesvirus infection, making them potential antiviral targets. Here, we present the 3.7-Å-resolution structure of the VZV A-capsid and define the molecular determinants underpinning the assembly of this complicated viral machinery. Overall, the VZV capsid has a similar architecture to that of other known herpesviruses. The major capsid protein (MCP) assembles into pentons and hexons, forming extensive intra- and inter-capsomer interaction networks that are further secured by the small capsid protein (SCP) and the heterotriplex. The structure reveals a pocket beneath the floor of MCP that could potentially be targeted by antiviral inhibitors. In addition, we identified two alphaherpesvirus-specific structural features in SCP and Tri1 proteins. These observations highlight the divergence of different herpesviruses and provide an important basis for developing antiviral drugs.

Date: 2020
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DOI: 10.1038/s41467-020-18537-y

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