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

doi:10.1038/s41467-023-39942-z

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^*

^*此作品的通讯作者

CAS - Institute of Microbiology
University of Chinese Academy of Sciences
Tsinghua University
Shanxi Agricultural University
Chinese Academy of Sciences
Shanxi Academy of Advanced Research and Innovation
University of Macau
Chinese Center for Disease Control and Prevention
Southern University of Science and Technology
Beijing Life Science Academy

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29 引用（Scopus）

摘要

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.

源语言	英语
文章编号	4405
期刊	Nature Communications
卷	14
期	1
DOI	https://doi.org/10.1038/s41467-023-39942-z
出版状态	已出版 - 12月 2023
已对外发布	是

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Zhao, Z., Xie, Y., Bai, B., Luo, C., Zhou, J., Li, W., Meng, Y., Li, L., Li, D., Li, X., Li, X., Wang, X., Sun, J., Xu, Z., Sun, Y., Zhang, W., Fan, Z., Zhao, X., Wu, L., ... Qi, J. (2023). Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants. Nature Communications, 14(1), 文章 4405. https://doi.org/10.1038/s41467-023-39942-z

@article{ed43ad96ccf044f98f59564f33feb93d,

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

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.",

author = "Zhennan Zhao and Yufeng Xie and Bin Bai and Chunliang Luo and Jingya Zhou and Weiwei Li and Yumin Meng and Linjie Li and Dedong Li and Xiaomei Li and Xiaoxiong Li and Xiaoyun Wang and Junqing Sun and Zepeng Xu and Yeping Sun and Wei Zhang and Zheng Fan and Xin Zhao and Linhuan Wu and Juncai Ma and Li, \{Odel Y.\} and Guijun Shang and Yan Chai and Kefang Liu and Peiyi Wang and Gao, \{George F.\} and Jianxun Qi",

note = "Publisher Copyright: {\textcopyright} 2023, The Author(s).",

year = "2023",

month = dec,

doi = "10.1038/s41467-023-39942-z",

language = "英语",

volume = "14",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Research",

number = "1",

}

Zhao, Z, Xie, Y, Bai, B, Luo, C, Zhou, J, Li, W, Meng, Y, Li, L, Li, D, Li, X, Li, X, Wang, X, Sun, J, Xu, Z, Sun, Y, Zhang, W, Fan, Z, Zhao, X, Wu, L, Ma, J, Li, OY, Shang, G, Chai, Y, Liu, K, Wang, P, Gao, GF & Qi, J 2023, 'Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants', Nature Communications, 卷 14, 号码 1, 4405. https://doi.org/10.1038/s41467-023-39942-z

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

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 -

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

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