Cryo-EM structure of a herpesvirus capsid at 3.1 Å

Shuai Yuan; Jialing Wang; Dongjie Zhu; Nan Wang; Qiang Gao; Wenyuan Chen; Hao Tang; Junzhi Wang; Xinzheng Zhang; Hongrong Liu; Zihe Rao; Xiangxi Wang

doi:10.1126/science.aao7283

Cryo-EM structure of a herpesvirus capsid at 3.1 Å

Science. 2018 Apr 6;360(6384):eaao7283. doi: 10.1126/science.aao7283.

Authors

Shuai Yuan^{1

2}, Jialing Wang^{1

2}, Dongjie Zhu^{1

3}, Nan Wang^{1

2}, Qiang Gao^{1

4}, Wenyuan Chen⁵, Hao Tang⁵, Junzhi Wang⁶, Xinzheng Zhang^{7

2}, Hongrong Liu⁸, Zihe Rao^{7

2

9

10

11}, Xiangxi Wang^{7

2}

Affiliations

¹ National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
² University of Chinese Academy of Sciences, Beijing, 100049, China.
³ School of Life Science, University of Science and Technology of China, Hefei, 230026, China.
⁴ Sinovac Biotech Co., Ltd., Beijing, 100085, China.
⁵ College of Physics and Information Science, Synergetic Innovation Center for Quantum Effects and Applications, Hunan Normal University, Changsha, 410081, Hunan, China.
⁶ National Institutes for Food and Drug Control, No. 2, Tiantanxili, Beijing, 100050, China. xiangxi@ibp.ac.cn hrliu@hunnu.edu.cn xzzhang@ibp.ac.cn wangjz@nicpbp.org.cn raozh@tsinghua.edu.cn.
⁷ National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. xiangxi@ibp.ac.cn hrliu@hunnu.edu.cn xzzhang@ibp.ac.cn wangjz@nicpbp.org.cn raozh@tsinghua.edu.cn.
⁸ College of Physics and Information Science, Synergetic Innovation Center for Quantum Effects and Applications, Hunan Normal University, Changsha, 410081, Hunan, China. xiangxi@ibp.ac.cn hrliu@hunnu.edu.cn xzzhang@ibp.ac.cn wangjz@nicpbp.org.cn raozh@tsinghua.edu.cn.
⁹ Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China.
¹⁰ State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300353, China.
¹¹ Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, 100084, China.

PMID: 29622627
DOI: 10.1126/science.aao7283

Abstract

Structurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we report the herpes simplex virus type 2 (HSV-2) capsid structure at 3.1 angstroms, which is built up of about 3000 proteins organized into three types of hexons (central, peripentonal, and edge), pentons, and triplexes. Both hexons and pentons contain the major capsid protein, VP5; hexons also contain a small capsid protein, VP26; and triplexes comprise VP23 and VP19C. Acting as core organizers, VP5 proteins form extensive intermolecular networks, involving multiple disulfide bonds (about 1500 in total) and noncovalent interactions, with VP26 proteins and triplexes that underpin capsid stability and assembly. Conformational adaptations of these proteins induced by their microenvironments lead to 46 different conformers that assemble into a massive quasisymmetric shell, exemplifying the structural and functional complexity of HSV.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Capsid / chemistry*
Capsid / ultrastructure
Capsid Proteins / chemistry*
Capsid Proteins / ultrastructure
Cryoelectron Microscopy
Herpesvirus 2, Human / chemistry*
Herpesvirus 2, Human / ultrastructure
Humans
Image Processing, Computer-Assisted

Substances

Capsid Proteins