Structures of pseudorabies virus capsids

Guosong Wang, Zhenghui Zha, Pengfei Huang, Hui Sun, Yang Huang, Maozhou He, Tian Chen, Lina Lin, Zhenqin Chen, Zhibo Kong, Yuqiong Que, Tingting Li, Ying Gu, Hai Yu, Jun Zhang, Qingbing Zheng (), Yixin Chen (), Shaowei Li () and Ningshao Xia ()
Additional contact information
Guosong Wang: Xiamen University
Zhenghui Zha: Xiamen University
Pengfei Huang: Xiamen University
Hui Sun: Xiamen University
Yang Huang: Xiamen University
Maozhou He: Xiamen University
Tian Chen: Xiamen University
Lina Lin: Xiamen University
Zhenqin Chen: Xiamen University
Zhibo Kong: Xiamen University
Yuqiong Que: Xiamen University
Tingting Li: Xiamen University
Ying Gu: Xiamen University
Hai Yu: Xiamen University
Jun Zhang: Xiamen University
Qingbing Zheng: Xiamen University
Yixin Chen: Xiamen University
Shaowei Li: Xiamen University
Ningshao Xia: Xiamen University

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral encephalitis caused by PRV infection, suggesting that PRV may be able to overcome the species barrier to infect humans. To date, there is no available therapeutic for PRV infection. Here, we report the near-atomic structures of the PRV A-capsid and C-capsid, and illustrate the interaction that occurs between these subunits. We show that the C-capsid portal complex is decorated with capsid-associated tegument complexes. The PRV capsid structure is highly reminiscent of other α-herpesviruses, with some additional structural features of β- and γ-herpesviruses. These results illustrate the structure of the PRV capsid and elucidate the underlying assembly mechanism at the molecular level. This knowledge may be useful for the development of oncolytic agents or specific therapeutics against this arm of the herpesvirus family.

Date: 2022
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DOI: 10.1038/s41467-022-29250-3

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