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Structure (London, England : 1993)2022; 30(10); 1432-1442.e4; doi: 10.1016/j.str.2022.07.005

Structural insights into the binding of SARS-CoV-2, SARS-CoV, and hCoV-NL63 spike receptor-binding domain to horse ACE2.

Abstract: Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV-2, and human coronavirus (hCoV)-NL63 utilize ACE2 as the functional receptor for cell entry, which leads to zoonotic infection. Horses (Equus caballus) attracted our attention because the spike protein receptor-binding domains (RBDs) of SARS-CoV-2 and SARS-CoV-2-related coronaviruses bind equine ACE2 (eACE2) with high affinity. Here we show that eACE2 binds the RBDs of these three coronaviruses and also SARS-CoV-2 variants but with lower affinities compared with human ACE2 (hACE2). Structural analysis and mutation assays indicated that eACE2-H41 accounts for the lower binding affinity of eACE2 to the RBDs of SARS-CoV-2 variants (Alpha, Beta, and Gamma), SARS-CoV, and hCoV-NL63. Pseudovirus infection assays showed that the SARS-CoV-2 Delta strain (B.1.617.2) displayed a significantly increased infection efficiency in eACE2-expressing HeLa cells. Our results reveal the molecular basis of eACE2 binding to the RBDs of SARS-CoV, SARS-CoV-2, and hCoV-NL63, which provides insights into the potential animal transmission of these ACE2-dependent coronaviruses.
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Publication Date: 2022-08-01 PubMed ID: 35917815PubMed Central: PMC9341007DOI: 10.1016/j.str.2022.07.005Google Scholar: Lookup
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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.

The research investigates how SARS-CoV-2, SARS-CoV, and hCoV-NL63, which are types of coronaviruses, bind to the ACE2 receptor in horses. The study provides insights into how these viruses interact with the ACE2 receptor in horses, the potential for transmission of these ACE2-dependent coronaviruses to animals, and the variations that impact this transmission.

Key Findings

  • The study focused on understanding the binding of three different coronaviruses (SARS-CoV-2, SARS-CoV, and hCoV-NL63) to ACE2 receptors in horses (eACE2). The role of ACE2 in these coronaviruses is crucial as they use ACE2 as a functional receptor for cell entry, leading to zoonotic infection.
  • The researchers found that these three coronaviruses bind to eACE2, albeit with lower affinities compared to human ACE2 (hACE2). This means that while the viruses can bind to the horse ACE2 receptors, they are more likely to bind to the human ACE2 receptors.

Molecular Basis of Binding and Potential Impacts

  • A deeper structural analysis and mutation assays showed that the lower binding affinity in horses is due to eACE2-H41—a mutation in the horse ACE2 receptor. This mutation decreases the ability of the RBDs of these coronaviruses and SARS-CoV-2 variants (Alpha, Beta, and Gamma) to bind to the horse ACE2 receptor.
  • They also conducted pseudovirus infection assays, finding that the SARS-CoV-2 Delta strain showed a significant increase in infection efficiency in HeLa cells that expressed eACE2. HeLa cells are a type of human cell line used in scientific research.
  • These findings unlock important understanding about the molecular basis of how coronaviruses bind to receptors in horses, giving key insights into the potential for these ACE2-dependent coronaviruses to be transmitted to animals. Understanding these dynamics can help strategize measures to prevent cross-species transmission.

Cite This Article

APA
Lan J, Chen P, Liu W, Ren W, Zhang L, Ding Q, Zhang Q, Wang X, Ge J. (2022). Structural insights into the binding of SARS-CoV-2, SARS-CoV, and hCoV-NL63 spike receptor-binding domain to horse ACE2. Structure, 30(10), 1432-1442.e4. https://doi.org/10.1016/j.str.2022.07.005

Publication

Structure (London, England : 1993)
ISSN: 1878-4186
NlmUniqueID: 101087697
Country: United States
Language: English
Volume: 30
Issue: 10
Pages: 1432-1442.e4
PII: S0969-2126(22)00274-X

Researcher Affiliations

Lan, Jun
  • The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China.
Chen, Peng
  • Comprehensive AIDS Research Center, Beijing Advanced Innovation Center for Structural Biology, School of Medicine and Vanke School of Public Health, Tsinghua University, Beijing, China.
Liu, Weiming
  • Department of Critical Care Medicine, Beijing Boai Hospital, China Rehabilitation Research Centre, No. 10 Jiaomen Beilu, Fengtai District, Beijing 100068, China.
Ren, Wenlin
  • Center for Infectious Disease Research, Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University, Beijing, China.
Zhang, Linqi
  • Comprehensive AIDS Research Center, Beijing Advanced Innovation Center for Structural Biology, School of Medicine and Vanke School of Public Health, Tsinghua University, Beijing, China.
Ding, Qiang
  • Center for Infectious Disease Research, Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University, Beijing, China.
Zhang, Qi
  • Comprehensive AIDS Research Center, Beijing Advanced Innovation Center for Structural Biology, School of Medicine and Vanke School of Public Health, Tsinghua University, Beijing, China. Electronic address: zhangqi2013@mail.tsinghua.edu.cn.
Wang, Xinquan
  • The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China. Electronic address: xinquanwang@mail.tsinghua.edu.cn.
Ge, Jiwan
  • The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China; Tsinghua-Peking Center for Life Sciences, Beijing, China. Electronic address: gejw@mail.tsinghua.edu.cn.

MeSH Terms

  • Angiotensin-Converting Enzyme 2
  • Animals
  • COVID-19
  • Coronavirus NL63, Human
  • HeLa Cells
  • Horses
  • Humans
  • Peptidyl-Dipeptidase A / genetics
  • Peptidyl-Dipeptidase A / metabolism
  • SARS-CoV-2
  • Spike Glycoprotein, Coronavirus / genetics

Conflict of Interest Statement

Declaration of interests The authors declare no competing interests.

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