Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants
Zhao，Zhennan1,2; Xie，Yufeng1,3; Bai，Bin1,2; Luo，Chunliang1,4; Zhou，Jingya2,5; Li，Weiwei1,2; Meng，Yumin1,2; Li，Linjie1,2; Li，Dedong1; Li，Xiaomei6; Li，Xiaoxiong6; Wang，Xiaoyun1; Sun，Junqing1,4; Xu，Zepeng1,7; Sun，Yeping1; Zhang，Wei1; Fan，Zheng1; Zhao，Xin1; Wu，Linhuan8; Ma，Juncai8; Li，Odel Y.9; Shang，Guijun6; Chai，Yan1; Liu，Kefang1; Wang，Peiyi10; Gao，George F.1,2,5; Qi，Jianxun1,2,11
|Corresponding Author||Liu，Kefang; Wang，Peiyi; Gao，George F.; Qi，Jianxun|
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.
NI Journal Papers ; NI论文
National Key R&D Program of China["2023YFC3041500","2021YFC2301401"] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XD29010202] ; National Natural Science Foundation of China ; Special Program of China National Tobacco Corporation ; China Postdoctoral Science Foundation[2022T150688] ; Young Elite Scientists Sponsorship Program by CAST[2021QNRC001]
|WOS Research Area|
Science & Technology - Other Topics
|WOS Accession No|
Cited Times [WOS]:1
|Document Type||Journal Article|
|Department||Department of Biology|
1.CAS Key Laboratory of Pathogen Microbiology and Immunology,Institute of Microbiology,Chinese Academy of Sciences,Beijing,China
2.University of Chinese Academy of Sciences,Beijing,China
3.Department of Basic Medical Sciences,School of Medicine,Tsinghua University,Beijing,China
4.College of Veterinary Medicine,Shanxi Agricultural University,Jinzhong,China
5.Research Network of Immunity and Health (RNIH),Beijing Institutes of Life Science,Chinese Academy of Sciences,Beijing,China
6.Shanxi Academy of Advanced Research and Innovation,Taiyuan,China
7.Faculty of Health Sciences,University of Macau,Macao
8.Chinese National Microbiology Data Center (NMDC),Institute of Microbiology,Chinese Academy of Sciences,Beijing,China
9.NHC Key Laboratory of Parasite and Vector Biology,National Institute of Parasitic Diseases,Chinese Center for Disease Control and Prevention,Shanghai,China
10.Cryo-EM Center,Department of Biology,Southern University of Science and Technology,Shenzhen,China
11.Beijing Life Science Academy,Beijing,China
|Corresponding Author Affilication||Department of Biology; School of Life Sciences|
Zhao，Zhennan,Xie，Yufeng,Bai，Bin,et al. Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants[J]. Nature Communications,2023,14(1).
Zhao，Zhennan.,Xie，Yufeng.,Bai，Bin.,Luo，Chunliang.,Zhou，Jingya.,...&Qi，Jianxun.(2023).Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants.Nature Communications,14(1).
Zhao，Zhennan,et al."Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants".Nature Communications 14.1(2023).
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