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Capsid protein structure in Zika virus reveals the flavivirus assembly process

Author

Listed:
  • Ter Yong Tan

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Guntur Fibriansah

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Victor A. Kostyuchenko

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Thiam-Seng Ng

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Xin-Xiang Lim

    (National University of Singapore)

  • Shuijun Zhang

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Xin-Ni Lim

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Jiaqi Wang

    (Duke–National University of Singapore Medical School
    National University of Singapore)

  • Jian Shi

    (National University of Singapore)

  • Marc C. Morais

    (University of Texas Medical Branch)

  • Davide Corti

    (Humabs BioMed SA, a subsidiary of Vir Biotechnology, Inc.)

  • Shee-Mei Lok

    (Duke–National University of Singapore Medical School
    National University of Singapore)

Abstract

Structures of flavivirus (dengue virus and Zika virus) particles are known to near-atomic resolution and show detailed structure and arrangement of their surface proteins (E and prM in immature virus or M in mature virus). By contrast, the arrangement of the capsid proteins:RNA complex, which forms the core of the particle, is poorly understood, likely due to inherent dynamics. Here, we stabilize immature Zika virus via an antibody that binds across the E and prM proteins, resulting in a subnanometer resolution structure of capsid proteins within the virus particle. Fitting of the capsid protein into densities shows the presence of a helix previously thought to be removed via proteolysis. This structure illuminates capsid protein quaternary organization, including its orientation relative to the lipid membrane and the genomic RNA, and its interactions with the transmembrane regions of the surface proteins. Results show the capsid protein plays a central role in the flavivirus assembly process.

Suggested Citation

  • Ter Yong Tan & Guntur Fibriansah & Victor A. Kostyuchenko & Thiam-Seng Ng & Xin-Xiang Lim & Shuijun Zhang & Xin-Ni Lim & Jiaqi Wang & Jian Shi & Marc C. Morais & Davide Corti & Shee-Mei Lok, 2020. "Capsid protein structure in Zika virus reveals the flavivirus assembly process," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14647-9
    DOI: 10.1038/s41467-020-14647-9
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    Cited by:

    1. Sarah Goellner & Giray Enkavi & Vibhu Prasad & Solène Denolly & Sungmin Eu & Giulia Mizzon & Leander Witte & Waldemar Kulig & Zina M. Uckeley & Teresa M. Lavacca & Uta Haselmann & Pierre-Yves Lozach &, 2023. "Zika virus prM protein contains cholesterol binding motifs required for virus entry and assembly," Nature Communications, Nature, vol. 14(1), pages 1-20, December.
    2. Guang-Yuan Song & Xing-Yao Huang & Meng-Jiao He & Hang-Yu Zhou & Rui-Ting Li & Ying Tian & Yan Wang & Meng-Li Cheng & Xiang Chen & Rong-Rong Zhang & Chao Zhou & Jia Zhou & Xian-Yang Fang & Xiao-Feng L, 2023. "A single amino acid substitution in the capsid protein of Zika virus contributes to a neurovirulent phenotype," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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