Résumé
SARS-CoV-2 (Severe Acute Respiratory Syndrome coronavirus 2) has been reported to infect domesticated animals in a species-specific manner, where cats were susceptible but not dogs. Using the recently published crystal structure of the SARS-CoV-2 spike protein complexed with the human host cell receptor angiotensin converting enzyme 2 (ACE2), we characterized the structure and evolution of ACE2 in several of these species and identify a single interacting amino acid residue conserved between human and Felidae ACE2 but not in Canidae that correlates with virus susceptibility. Using computational analyses we describe how this site likely affects ACE2 targeting by the virus. Thus, we highlight how evolution-based approaches can be used to form hypotheses and study animal transmission of such viruses in the future.
| Langue d'origine | English |
|---|---|
| Pages (de-à) | 109-113 |
| Nombre de pages | 5 |
| Journal | Evolution, Medicine and Public Health |
| Volume | 2020 |
| Numéro de publication | 1 |
| DOI | |
| Statut de publication | Published - 2020 |
Note bibliographique
Funding Information:This work was supported by a Discovery Grant from the Natural Science and Engineering Research Council of Canada (NSERC) (RGPIN-04034 to G.D.), and S.M. is supported by a Killam Pre-Doctoral Award, as well as a Nova Scotia Graduate Scholarship and Dalhousie University’s Presidents Award.
Publisher Copyright:
© 2020 Oxford University Press. All rights reserved.
ASJC Scopus Subject Areas
- Medicine (miscellaneous)
- Ecology, Evolution, Behavior and Systematics
- Health, Toxicology and Mutagenesis