Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component

Jialing Wang, Shuai Yuan, Dongjie Zhu, Hao Tang, Nan Wang, Wenyuan Chen, Qiang Gao, Yuhua Li, Junzhi Wang, Hongrong Liu (), Xinzheng Zhang (), Zihe Rao () and Xiangxi Wang ()
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Jialing Wang: Chinese Academy of Science
Shuai Yuan: Chinese Academy of Science
Dongjie Zhu: Chinese Academy of Science
Hao Tang: Hunan Normal University
Nan Wang: Chinese Academy of Science
Wenyuan Chen: Hunan Normal University
Qiang Gao: Chinese Academy of Science
Yuhua Li: National Institutes for Food and Drug Control
Junzhi Wang: National Institutes for Food and Drug Control
Hongrong Liu: Hunan Normal University
Xinzheng Zhang: Chinese Academy of Science
Zihe Rao: Chinese Academy of Science
Xiangxi Wang: Chinese Academy of Science

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: Abstract Herpes simplex viruses (HSVs) cause human oral and genital ulcer diseases. Patients with HSV-2 have a higher risk of acquiring a human immunodeficiency virus infection. HSV-2 is a member of the α-herpesvirinae subfamily that together with the β- and γ-herpesvirinae subfamilies forms the Herpesviridae family. Here, we report the cryo-electron microscopy structure of the HSV-2 C-capsid with capsid-vertex-specific component (CVSC) that was determined at 3.75 Å using a block-based reconstruction strategy. We present atomic models of multiple conformers for the capsid proteins (VP5, VP23, VP19C, and VP26) and CVSC. Comparison of the HSV-2 homologs yields information about structural similarities and differences between the three herpesviruses sub-families and we identify α-herpesvirus-specific structural features. The hetero-pentameric CVSC, consisting of a UL17 monomer, a UL25 dimer and a UL36 dimer, is bound tightly by a five-helix bundle that forms extensive networks of subunit contacts with surrounding capsid proteins, which reinforce capsid stability.

Date: 2018
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DOI: 10.1038/s41467-018-06078-4

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