Binding and structural basis of equine ACE2 to RBDs from SARS-CoV, SARS-CoV-2 and related coronaviruses

Zepeng Xu, Xinrui Kang, Pu Han, Pei Du, Linjie Li, Anqi Zheng, Chuxia Deng, Jianxun Qi, Xin Zhao, Qihui Wang (), Kefang Liu () and George Fu Gao
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Zepeng Xu: Chinese Academy of Sciences
Xinrui Kang: Chinese Academy of Sciences
Pu Han: Chinese Academy of Sciences
Pei Du: Chinese Academy of Sciences
Linjie Li: Chinese Academy of Sciences
Anqi Zheng: Chinese Academy of Sciences
Chuxia Deng: University of Macau
Jianxun Qi: Chinese Academy of Sciences
Xin Zhao: Chinese Academy of Sciences
Qihui Wang: Chinese Academy of Sciences
Kefang Liu: Chinese Academy of Sciences
George Fu Gao: Chinese Academy of Sciences

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract The origin and host range of SARS-CoV-2, the causative agent of coronavirus disease 2019 (COVID-19), are important scientific questions as they might provide insight into understanding of the potential future spillover to infect humans. Here, we tested the binding between equine angiotensin converting enzyme 2 (eqACE2) and the receptor binding domains (RBDs) of SARS-CoV, SARS-CoV-2 prototype (PT) and variant of concerns (VOCs), as well as their close relatives bat-origin coronavirus (CoV) RaTG13 and pangolin-origin CoVs GX/P2V/2017 and GD/1/2019. We also determined the crystal structures of eqACE2/RaTG13-RBD, eqACE2/SARS-CoV-2 PT-RBD and eqACE2/Omicron BA.1-RBD. We identified S494 of SARS-COV-2 PT-RBD as an important residue in the eqACE2/SARS-COV-2 PT-RBD interaction and found that N501Y, the commonly recognized enhancing mutation, attenuated the binding affinity with eqACE2. Our work demonstrates that horses are potential targets for SARS-CoV-2 and highlights the importance of continuous surveillance on SARS-CoV-2 and related CoVs to prevent spillover events.

Date: 2022
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DOI: 10.1038/s41467-022-31276-6

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