Nature Communications (Jul 2023)
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,
- Jianxun Qi
Affiliations
- Zhennan Zhao
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Yufeng Xie
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Bin Bai
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Chunliang Luo
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Jingya Zhou
- University of Chinese Academy of Sciences
- Weiwei Li
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Yumin Meng
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Linjie Li
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Dedong Li
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Xiaomei Li
- Shanxi Academy of Advanced Research and Innovation
- Xiaoxiong Li
- Shanxi Academy of Advanced Research and Innovation
- Xiaoyun Wang
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Junqing Sun
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Zepeng Xu
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Yeping Sun
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Wei Zhang
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Zheng Fan
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Xin Zhao
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Linhuan Wu
- Chinese National Microbiology Data Center (NMDC), Institute of Microbiology, Chinese Academy of Sciences
- Juncai Ma
- Chinese National Microbiology Data Center (NMDC), Institute of Microbiology, Chinese Academy of Sciences
- Odel Y. Li
- NHC Key Laboratory of Parasite and Vector Biology, National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention
- Guijun Shang
- Shanxi Academy of Advanced Research and Innovation
- Yan Chai
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Kefang Liu
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Peiyi Wang
- Cryo-EM Center, Department of Biology, Southern University of Science and Technology
- George F. Gao
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- Jianxun Qi
- CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
- DOI
- https://doi.org/10.1038/s41467-023-39942-z
- Journal volume & issue
-
Vol. 14,
no. 1
pp. 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.
