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Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure

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  • Lihong Chen

    (Chinese Academy of Sciences
    Chinese Academy of Agricultural Sciences
    University of Chinese Academy of Sciences)

  • Ming Wang

    (Chinese Academy of Agricultural Sciences)

  • Dongjie Zhu

    (Chinese Academy of Sciences
    University of Science and Technology of China)

  • Zhenzhao Sun

    (Chinese Academy of Agricultural Sciences)

  • Jun Ma

    (Chinese Academy of Sciences)

  • Jinglin Wang

    (Yunnan Animal Science and Veterinary Institute)

  • Lingfei Kong

    (Chinese Academy of Sciences)

  • Shida Wang

    (Chinese Academy of Agricultural Sciences)

  • Zaisi Liu

    (Chinese Academy of Agricultural Sciences)

  • Lili Wei

    (Chinese Academy of Agricultural Sciences)

  • Yuwen He

    (Yunnan Animal Science and Veterinary Institute)

  • Jingfei Wang

    (Chinese Academy of Agricultural Sciences)

  • Xinzheng Zhang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

Abstract

Alphaviruses are enveloped RNA viruses that contain several human pathogens. Due to intrinsic heterogeneity of alphavirus particles, a high resolution structure of the virion is currently lacking. Here we provide a 3.5 Å cryo-EM structure of Sindbis virus, using block based reconstruction method that overcomes the heterogeneity problem. Our structural analysis identifies a number of conserved residues that play pivotal roles in the virus life cycle. We identify a hydrophobic pocket in the subdomain D of E2 protein that is stabilized by an unknown pocket factor near the viral membrane. Residues in the pocket are conserved in different alphaviruses. The pocket strengthens the interactions of the E1/E2 heterodimer and may facilitate virus assembly. Our study provides structural insights into alphaviruses that may inform the design of drugs and vaccines.

Suggested Citation

  • Lihong Chen & Ming Wang & Dongjie Zhu & Zhenzhao Sun & Jun Ma & Jinglin Wang & Lingfei Kong & Shida Wang & Zaisi Liu & Lili Wei & Yuwen He & Jingfei Wang & Xinzheng Zhang, 2018. "Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07704-x
    DOI: 10.1038/s41467-018-07704-x
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    Cited by:

    1. Pan Yang & Wanyu Li & Xiaoyi Fan & Junhua Pan & Colin J. Mann & Haley Varnum & Lars E. Clark & Sarah A. Clark & Adrian Coscia & Himanish Basu & Katherine Nabel Smith & Vesna Brusic & Jonathan Abraham, 2024. "Structural basis for VLDLR recognition by eastern equine encephalitis virus," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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