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

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, Wei Zhang, Zheng Fan, Xin Zhao, Linhuan Wu, Juncai Ma, Odel Y. Li, Guijun Shang, Yan Chai, Kefang Liu (), Peiyi Wang (), George F. Gao () and Jianxun Qi ()
Additional contact information
Zhennan Zhao: Chinese Academy of Sciences
Yufeng Xie: Chinese Academy of Sciences
Bin Bai: Chinese Academy of Sciences
Chunliang Luo: Chinese Academy of Sciences
Jingya Zhou: University of Chinese Academy of Sciences
Weiwei Li: Chinese Academy of Sciences
Yumin Meng: Chinese Academy of Sciences
Linjie Li: 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
Zepeng Xu: Chinese Academy of Sciences
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
Jianxun Qi: Chinese Academy of Sciences

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-39942-z

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