TY - JOUR
T1 - Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants
AU - Zhao, Zhennan
AU - Xie, Yufeng
AU - Bai, Bin
AU - Luo, Chunliang
AU - Zhou, Jingya
AU - Li, Weiwei
AU - Meng, Yumin
AU - Li, Linjie
AU - Li, Dedong
AU - Li, Xiaomei
AU - Li, Xiaoxiong
AU - Wang, Xiaoyun
AU - Sun, Junqing
AU - Xu, Zepeng
AU - Sun, Yeping
AU - Zhang, Wei
AU - Fan, Zheng
AU - Zhao, Xin
AU - Wu, Linhuan
AU - Ma, Juncai
AU - Li, Odel Y.
AU - Shang, Guijun
AU - Chai, Yan
AU - Liu, Kefang
AU - Wang, Peiyi
AU - Gao, George F.
AU - Qi, Jianxun
N1 - Publisher Copyright:
© 2023, The Author(s).
PY - 2023/12
Y1 - 2023/12
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/85165411198
U2 - 10.1038/s41467-023-39942-z
DO - 10.1038/s41467-023-39942-z
M3 - 文章
C2 - 37479708
AN - SCOPUS:85165411198
SN - 2041-1723
VL - 14
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 4405
ER -