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.
【초록키워드】 COVID-19, coronavirus disease, SARS-CoV-2, Coronavirus disease 2019, coronavirus, Mutation, SARS-CoV, variant, omicron, angiotensin converting enzyme, binding affinity, Receptor binding domain, Surveillance, N501Y, humans, VOCs, RaTG13, CoV, host range, target, crystal structure, binding, Interaction, angiotensin, RBDs, crystal structures, causative agent, continuous surveillance, enzyme, residue, CoVs, equine, receptor binding domains, infect, Prevent, highlight, tested, events, question, the binding affinity, 【제목키워드】 SARS-CoV-2, ACE2, SARS-CoV, RBD, equine, coronavirus,