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Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2

The susceptibility of the white-tailed deer (WTD; Odocoileus virginianus) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has highlighted cervids as coronavirus reservoirs. This study aimed to evaluate the angiotensin-converting enzyme 2 (ACE2) residues which bind the spike protein o...

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Detalles Bibliográficos
Autor principal: Lopes, Luciano Rodrigo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10139662/
https://www.ncbi.nlm.nih.gov/pubmed/37106170
http://dx.doi.org/10.1007/s10393-023-01632-z
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author Lopes, Luciano Rodrigo
author_facet Lopes, Luciano Rodrigo
author_sort Lopes, Luciano Rodrigo
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description The susceptibility of the white-tailed deer (WTD; Odocoileus virginianus) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has highlighted cervids as coronavirus reservoirs. This study aimed to evaluate the angiotensin-converting enzyme 2 (ACE2) residues which bind the spike protein of SARS-CoV-2 from 16 cervids to predict their potential susceptibility to SARS-CoV-2 infection. Eleven out of 16 species presented identical ACE2 key residues to WTD ACE2. Four cervids presented K31N, a variant associated with low SARS-CoV-2 susceptibility. Large herding of cervids with ACE2 key residues identical to that of the WTD can result in extensive reservoirs of SARS-CoV-2. Cervids as potential reservoirs could favor SARS-CoV-2 adaptation and the emergence of new coronavirus strains. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10393-023-01632-z.
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spelling pubmed-101396622023-04-28 Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2 Lopes, Luciano Rodrigo Ecohealth Short Communication The susceptibility of the white-tailed deer (WTD; Odocoileus virginianus) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has highlighted cervids as coronavirus reservoirs. This study aimed to evaluate the angiotensin-converting enzyme 2 (ACE2) residues which bind the spike protein of SARS-CoV-2 from 16 cervids to predict their potential susceptibility to SARS-CoV-2 infection. Eleven out of 16 species presented identical ACE2 key residues to WTD ACE2. Four cervids presented K31N, a variant associated with low SARS-CoV-2 susceptibility. Large herding of cervids with ACE2 key residues identical to that of the WTD can result in extensive reservoirs of SARS-CoV-2. Cervids as potential reservoirs could favor SARS-CoV-2 adaptation and the emergence of new coronavirus strains. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10393-023-01632-z. Springer US 2023-04-27 2023 /pmc/articles/PMC10139662/ /pubmed/37106170 http://dx.doi.org/10.1007/s10393-023-01632-z Text en © EcoHealth Alliance 2023 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Short Communication
Lopes, Luciano Rodrigo
Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2
title Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2
title_full Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2
title_fullStr Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2
title_full_unstemmed Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2
title_short Cervids ACE2 Residues that Bind the Spike Protein can Provide Susceptibility to SARS-CoV-2
title_sort cervids ace2 residues that bind the spike protein can provide susceptibility to sars-cov-2
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10139662/
https://www.ncbi.nlm.nih.gov/pubmed/37106170
http://dx.doi.org/10.1007/s10393-023-01632-z
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