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Home / Equine Research Bank / Nat Commun / Binding and structural basis of equine ACE2 to RBDs from SAR...
Nature communications2022; 13(1); 3547; doi: 10.1038/s41467-022-31276-6

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

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.
© 2022. The Author(s).
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Publication Date: 2022-06-21 PubMed ID: 35729237PubMed Central: PMC9210341DOI: 10.1038/s41467-022-31276-6Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research looked at the interaction between various coronavirus strains and the equine angiotensin converting enzyme 2 (eqACE2), determining that horses might be potential targets for these viruses including SARS-CoV-2.

Research Focus

  • The aim of this research was to better understand the host range and origin of SARS-CoV-2, along with other related coronaviruses. This is crucial to gain insight into potential future spillover scenarios where these viruses can infect humans.

Methodology

  • The researchers tested the bindings between eqACE2, which is a receptor found in horses, and the receptor binding domains (RBDs) of various versions of the severe acute respiratory syndrome coronaviruses SARS-CoV and SARS-Cov-2, including the prototype and variants of concern (VOCs).
  • They also tested bindings with RBDs found in other coronaviruses that originate from bats and pangolins.
  • The research team also used crystallography to determine the structural elements of these bindings.

Findings

  • Through these tests, the research team pinpointed the S494 on the SARS-CoV2 PT-RBD as a crucial residue that interacts with eqACE2.
  • Interestingly, they also found that the mutation N501Y, which is widely recognized as enhancing the virus’ ability to bind with human cells, actually diminished the binding affinity with eqACE2.

Conclusions

  • The findings demonstrate that horses could be potential hosts for SARS-CoV-2 and other related coronaviruses.
  • This kind of research is crucial for ongoing surveillance of these viruses to prevent future spillover events that could potentially lead to outbreaks in the human population.

Cite This Article

APA
Xu Z, Kang X, Han P, Du P, Li L, Zheng A, Deng C, Qi J, Zhao X, Wang Q, Liu K, Gao GF. (2022). Binding and structural basis of equine ACE2 to RBDs from SARS-CoV, SARS-CoV-2 and related coronaviruses. Nat Commun, 13(1), 3547. https://doi.org/10.1038/s41467-022-31276-6

Publication

Nature communications
ISSN: 2041-1723
NlmUniqueID: 101528555
Country: England
Language: English
Volume: 13
Issue: 1
Pages: 3547
PII: 3547

Researcher Affiliations

Xu, Zepeng
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
  • Faculty of Health Sciences, University of Macau, Macau SAR, 999078, China.
Kang, Xinrui
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
  • Savaid Medical School, University of Chinese Academy of Sciences, Beijing, 100049, China.
Han, Pu
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Du, Pei
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Li, Linjie
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
  • University of Chinese Academy of Sciences, Beijing, 100049, China.
Zheng, Anqi
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
  • University of Chinese Academy of Sciences, Beijing, 100049, China.
Deng, Chuxia
  • Faculty of Health Sciences, University of Macau, Macau SAR, 999078, China.
Qi, Jianxun
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
  • University of Chinese Academy of Sciences, Beijing, 100049, China.
Zhao, Xin
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Wang, Qihui
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. wangqihui@im.ac.cn.
  • University of Chinese Academy of Sciences, Beijing, 100049, China. wangqihui@im.ac.cn.
Liu, Kefang
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. Liukf@im.ac.cn.
Gao, George Fu
  • CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.

MeSH Terms

  • Angiotensin-Converting Enzyme 2
  • Animals
  • COVID-19
  • Horses
  • Peptidyl-Dipeptidase A / metabolism
  • Protein Binding
  • SARS-CoV-2 / genetics
  • Spike Glycoprotein, Coronavirus / metabolism

Conflict of Interest Statement

The authors declare no competing interests.

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