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Structures of pseudorabies virus capsids

Author

Listed:
  • Guosong Wang

    (Xiamen University
    Xiamen University)

  • Zhenghui Zha

    (Xiamen University
    Xiamen University)

  • Pengfei Huang

    (Xiamen University
    Xiamen University)

  • Hui Sun

    (Xiamen University
    Xiamen University)

  • Yang Huang

    (Xiamen University
    Xiamen University)

  • Maozhou He

    (Xiamen University
    Xiamen University)

  • Tian Chen

    (Xiamen University
    Xiamen University)

  • Lina Lin

    (Xiamen University
    Xiamen University)

  • Zhenqin Chen

    (Xiamen University
    Xiamen University)

  • Zhibo Kong

    (Xiamen University
    Xiamen University)

  • Yuqiong Que

    (Xiamen University
    Xiamen University)

  • Tingting Li

    (Xiamen University
    Xiamen University)

  • Ying Gu

    (Xiamen University
    Xiamen University)

  • Hai Yu

    (Xiamen University
    Xiamen University)

  • Jun Zhang

    (Xiamen University
    Xiamen University)

  • Qingbing Zheng

    (Xiamen University
    Xiamen University)

  • Yixin Chen

    (Xiamen University
    Xiamen University)

  • Shaowei Li

    (Xiamen University
    Xiamen University)

  • Ningshao Xia

    (Xiamen University
    Xiamen University
    Chinese Academy of Medical Sciences)

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.

Suggested Citation

  • 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, 2022. "Structures of pseudorabies virus capsids," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29250-3
    DOI: 10.1038/s41467-022-29250-3
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    References listed on IDEAS

    as
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    2. Serban L. Ilca & Abhay Kotecha & Xiaoyu Sun & Minna M. Poranen & David I. Stuart & Juha T. Huiskonen, 2015. "Localized reconstruction of subunits from electron cryomicroscopy images of macromolecular complexes," Nature Communications, Nature, vol. 6(1), pages 1-8, December.
    3. Dongjie Zhu & Xiangxi Wang & Qianglin Fang & James L Etten & Michael G Rossmann & Zihe Rao & Xinzheng Zhang, 2018. "Pushing the resolution limit by correcting the Ewald sphere effect in single-particle Cryo-EM reconstructions," Nature Communications, Nature, vol. 9(1), pages 1-7, December.
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    5. Xinghong Dai & Danyang Gong & Hanyoung Lim & Jonathan Jih & Ting-Ting Wu & Ren Sun & Z. Hong Zhou, 2018. "Structure and mutagenesis reveal essential capsid protein interactions for KSHV replication," Nature, Nature, vol. 553(7689), pages 521-525, January.
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