tetano
Editor, Senior Moderator
Nat Commun
. 2022 Jun 21;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
Zepeng Xu[SUP] #[/SUP][SUP] 1 2 [/SUP], Xinrui Kang[SUP] #[/SUP][SUP] 1 3 [/SUP], Pu Han[SUP] #[/SUP][SUP] 1 [/SUP], Pei Du[SUP] #[/SUP][SUP] 1 [/SUP], Linjie Li[SUP] 1 4 [/SUP], Anqi Zheng[SUP] 1 4 [/SUP], Chuxia Deng[SUP] 2 [/SUP], Jianxun Qi[SUP] 1 4 [/SUP], Xin Zhao[SUP] 1 [/SUP], Qihui Wang[SUP] 5 6 [/SUP], Kefang Liu[SUP] 7 [/SUP], George Fu Gao[SUP] 1 [/SUP]
Affiliations
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 Jun 21;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
Zepeng Xu[SUP] #[/SUP][SUP] 1 2 [/SUP], Xinrui Kang[SUP] #[/SUP][SUP] 1 3 [/SUP], Pu Han[SUP] #[/SUP][SUP] 1 [/SUP], Pei Du[SUP] #[/SUP][SUP] 1 [/SUP], Linjie Li[SUP] 1 4 [/SUP], Anqi Zheng[SUP] 1 4 [/SUP], Chuxia Deng[SUP] 2 [/SUP], Jianxun Qi[SUP] 1 4 [/SUP], Xin Zhao[SUP] 1 [/SUP], Qihui Wang[SUP] 5 6 [/SUP], Kefang Liu[SUP] 7 [/SUP], George Fu Gao[SUP] 1 [/SUP]
Affiliations
- PMID: 35729237
- DOI: 10.1038/s41467-022-31276-6
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.