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Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants

Author

Listed:
  • Zhennan Zhao

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

  • Yufeng Xie

    (Chinese Academy of Sciences
    Tsinghua University)

  • Bin Bai

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

  • Chunliang Luo

    (Chinese Academy of Sciences
    Shanxi Agricultural University)

  • Jingya Zhou

    (University of Chinese Academy of Sciences
    Beijing Institutes of Life Science, Chinese Academy of Sciences)

  • Weiwei Li

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

  • Yumin Meng

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

  • Linjie Li

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

  • Dedong Li

    (Chinese Academy of Sciences)

  • Xiaomei Li

    (Shanxi Academy of Advanced Research and Innovation)

  • Xiaoxiong Li

    (Shanxi Academy of Advanced Research and Innovation)

  • Xiaoyun Wang

    (Chinese Academy of Sciences)

  • Junqing Sun

    (Chinese Academy of Sciences
    Shanxi Agricultural University)

  • Zepeng Xu

    (Chinese Academy of Sciences
    University of Macau)

  • Yeping Sun

    (Chinese Academy of Sciences)

  • Wei Zhang

    (Chinese Academy of Sciences)

  • Zheng Fan

    (Chinese Academy of Sciences)

  • Xin Zhao

    (Chinese Academy of Sciences)

  • Linhuan Wu

    (Institute of Microbiology, Chinese Academy of Sciences)

  • Juncai Ma

    (Institute of Microbiology, Chinese Academy of Sciences)

  • Odel Y. Li

    (National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention)

  • Guijun Shang

    (Shanxi Academy of Advanced Research and Innovation)

  • Yan Chai

    (Chinese Academy of Sciences)

  • Kefang Liu

    (Chinese Academy of Sciences)

  • Peiyi Wang

    (Southern University of Science and Technology)

  • George F. Gao

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences
    Beijing Institutes of Life Science, Chinese Academy of Sciences)

  • Jianxun Qi

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences
    Beijing Life Science Academy)

Abstract

Multiple SARS-CoV-2 Omicron sub-variants, such as BA.2, BA.2.12.1, BA.4, and BA.5, emerge one after another. BA.5 has become the dominant strain worldwide. Additionally, BA.2.75 is significantly increasing in some countries. Exploring their receptor binding and interspecies transmission risk is urgently needed. Herein, we examine the binding capacities of human and other 28 animal ACE2 orthologs covering nine orders towards S proteins of these sub-variants. The binding affinities between hACE2 and these sub-variants remain in the range as that of previous variants of concerns (VOCs) or interests (VOIs). Notably, R493Q reverse mutation enhances the bindings towards ACE2s from humans and many animals closely related to human life, suggesting an increased risk of cross-species transmission. Structures of S/hACE2 or RBD/hACE2 complexes for these sub-variants and BA.2 S binding to ACE2 of mouse, rat or golden hamster are determined to reveal the molecular basis for receptor binding and broader interspecies recognition.

Suggested Citation

  • Zhennan Zhao & Yufeng Xie & Bin Bai & Chunliang Luo & Jingya Zhou & Weiwei Li & Yumin Meng & Linjie Li & Dedong Li & Xiaomei Li & Xiaoxiong Li & Xiaoyun Wang & Junqing Sun & Zepeng Xu & Yeping Sun & W, 2023. "Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39942-z
    DOI: 10.1038/s41467-023-39942-z
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