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Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes

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  • Xiyong Song

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

  • Yuejun Shi

    (Huazhong Agricultural University
    Huazhong Agricultural University)

  • Wei Ding

    (Chinese Academy of Sciences)

  • Tongxin Niu

    (Chinese Academy of Sciences)

  • Limeng Sun

    (Huazhong Agricultural University
    Huazhong Agricultural University)

  • Yubei Tan

    (Huazhong Agricultural University
    Huazhong Agricultural University)

  • Yong Chen

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

  • Jiale Shi

    (Huazhong Agricultural University
    Huazhong Agricultural University)

  • Qiqi Xiong

    (Huazhong Agricultural University
    Huazhong Agricultural University)

  • Xiaojun Huang

    (Chinese Academy of Sciences)

  • Shaobo Xiao

    (Huazhong Agricultural University
    Huazhong Agricultural University)

  • Yanping Zhu

    (Chinese Academy of Sciences)

  • Chongyun Cheng

    (Chinese Academy of Sciences)

  • Zhen F. Fu

    (Huazhong Agricultural University
    Huazhong Agricultural University
    University of Georgia)

  • Zhi-Jie Liu

    (Kunming Medical University
    ShanghaiTech University)

  • Guiqing Peng

    (Huazhong Agricultural University
    Huazhong Agricultural University)

Abstract

Coronaviruses spike (S) glycoproteins mediate viral entry into host cells by binding to host receptors. However, how the S1 subunit undergoes conformational changes for receptor recognition has not been elucidated in Alphacoronavirus. Here, we report the cryo-EM structures of the HCoV-229E S trimer in prefusion state with two conformations. The activated conformation may pose the potential exposure of the S1-RBDs by decreasing of the interaction area between the S1-RBDs and the surrounding S1-NTDs and S1-RBDs compared to the closed conformation. Furthermore, structural comparison of our structures with the previously reported HCoV-229E S structure showed that the S trimers trended to open the S2 subunit from the closed conformation to open conformation, which could promote the transition from pre- to postfusion. Our results provide insights into the mechanisms involved in S glycoprotein-mediated Alphacoronavirus entry and have implications for vaccine and therapeutic antibody design.

Suggested Citation

  • Xiyong Song & Yuejun Shi & Wei Ding & Tongxin Niu & Limeng Sun & Yubei Tan & Yong Chen & Jiale Shi & Qiqi Xiong & Xiaojun Huang & Shaobo Xiao & Yanping Zhu & Chongyun Cheng & Zhen F. Fu & Zhi-Jie Liu , 2021. "Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20401-y
    DOI: 10.1038/s41467-020-20401-y
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    Cited by:

    1. Tiantian Yang & Aohua Wang & Di Nie & Weiwei Fan & Xiaohe Jiang & Miaorong Yu & Shiyan Guo & Chunliu Zhu & Gang Wei & Yong Gan, 2022. "Ligand-switchable nanoparticles resembling viral surface for sequential drug delivery and improved oral insulin therapy," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. David Chmielewski & Eric A. Wilson & Grigore Pintilie & Peng Zhao & Muyuan Chen & Michael F. Schmid & Graham Simmons & Lance Wells & Jing Jin & Abhishek Singharoy & Wah Chiu, 2023. "Structural insights into the modulation of coronavirus spike tilting and infectivity by hinge glycans," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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