ArticleStructure (London, England : 1993)2022
Structural insights into the binding of SARS-CoV-2, SARS-CoV, and hCoV-NL63 spike receptor-binding domain to horse ACE2.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Dual ACE2 epitope-based biomimetic receptors for selective sensing of SARS-CoV variants.Scientific reports · 2025Article
- Review
- Molecular mechanisms of RaTG13 and SARS-CoV-2 RBD bound to Rhinolophus affinis bat ACE2.Protein science : a publication of the Protein Society · 2025Article
- Bridging Cancer and COVID-19: The Complex Interplay of ACE2 and TMPRSS2.Cancer medicine · 2025Review
- Binding affinity between coronavirus spike protein and human ACE2 receptor.Computational and structural biotechnology journal · 2024Review
- Host-Directed Virus-Mimicking Particles Interacting with the ACE2 Receptor Competitively Block Coronavirus SARS-CoV-2 Entry.Nano letters · 2024Article
- Article
- Computational Drug Design Strategies for Fighting the COVID-19 Pandemic.Advances in experimental medicine and biology · 2024Article
- In Silico Analysis of Cross-Species Sequence Variability in Host Interferon Antiviral Pathway Proteins and SARS-CoV-2 Susceptibility.Zoonoses (Shannon, Ireland) · 2024Article
- Analysis of RBD-ACE2 interactions in livestock species as a factor in the spread of SARS-CoV-2 among animals.Veterinary and animal science · 2023Article
- Unravelling Antigenic Cross-Reactions toward the World of Coronaviruses: Extent of the Stability of Shared Epitopes and SARS-CoV-2 Anti-Spike Cross-Neutralizing Antibodies.Pathogens (Basel, Switzerland) · 2023Review
- Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range.PLoS pathogens · 2023Article
- SARS-CoV-2 Is More Efficient than HCoV-NL63 in Infecting a Small Subpopulation of ACE2+ Human Respiratory Epithelial Cells.Viruses · 2023Article
- Extracellular Vesicle-Based SARS-CoV-2 Vaccine.Vaccines · 2023Review
- Infection routes, invasion mechanisms, and drug inhibition pathways of human coronaviruses on the nervous system.Frontiers in neuroscience · 2023Review
- Hold your horses: The receptor-binding domains of SARS-CoV-2, SARS-CoV, and hCoV-NL63 bind equine ACE2.Structure (London, England : 1993) · 2022Article
- Advances in SARS-CoV-2 receptor-binding domain-based COVID-19 vaccines.Expert review of vaccinesReview
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9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.