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Diversity of ACE2 and its interaction with SARS-CoV-2 receptor binding domain

Jessie Low-Gan, Ruiqi Huang, Gabrielle Warner, Abigail Kelley, Duncan McGregor, View ORCID ProfileVaughn Smider
doi: https://doi.org/10.1101/2020.10.25.354548
Jessie Low-Gan
1San Diego Jewish Academy, San Diego, CA 92130
2Applied Biomedical Science Institute, San Diego, CA 92127
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Ruiqi Huang
2Applied Biomedical Science Institute, San Diego, CA 92127
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Gabrielle Warner
2Applied Biomedical Science Institute, San Diego, CA 92127
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Abigail Kelley
2Applied Biomedical Science Institute, San Diego, CA 92127
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Duncan McGregor
2Applied Biomedical Science Institute, San Diego, CA 92127
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Vaughn Smider
2Applied Biomedical Science Institute, San Diego, CA 92127
3The Scripps Research Institute, La Jolla, CA 92037
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  • ORCID record for Vaughn Smider
  • For correspondence: vaughn.smider@absinstitute.org
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Abstract

COVID-19, the clinical syndrome caused by the SARS-CoV-2 virus, has rapidly spread globally causing tens of millions of infections and over a million deaths. The potential animal reservoirs for SARS-CoV-2 are currently unknown, however sequence analysis has provided plausible potential candidate species. SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection. We analyzed the binding surface of ACE2 from several important animal species to begin to understand the parameters for the ACE2 recognition by the SARS-CoV-2 spike protein receptor binding domain (RBD). We employed Shannon entropy analysis to determine the variability of ACE2 across its sequence and particularly in its RBD interacting region, and assessed differences between various species’ ACE2 and human ACE2. As cattle are a known reservoir for coronaviruses with previous human zoonotic transfer, and has a relatively divergent ACE2 sequence, we compared the binding kinetics of bovine and human ACE2 to SARS-CoV-2 RBD. This revealed a nanomolar binding affinity for bovine ACE2 but an approximate ten-fold reduction of binding compared to human ACE2. Since cows have been experimentally infected by SARS-CoV-2, this lower affinity sets a threshold for sequences with lower homology to human ACE2 to be able to serve as a productive viral receptor for SARS-CoV-2.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • minor grammatical errors have been corrected

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted November 04, 2020.
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Diversity of ACE2 and its interaction with SARS-CoV-2 receptor binding domain
Jessie Low-Gan, Ruiqi Huang, Gabrielle Warner, Abigail Kelley, Duncan McGregor, Vaughn Smider
bioRxiv 2020.10.25.354548; doi: https://doi.org/10.1101/2020.10.25.354548
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Diversity of ACE2 and its interaction with SARS-CoV-2 receptor binding domain
Jessie Low-Gan, Ruiqi Huang, Gabrielle Warner, Abigail Kelley, Duncan McGregor, Vaughn Smider
bioRxiv 2020.10.25.354548; doi: https://doi.org/10.1101/2020.10.25.354548

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