Comparative ACE2 variation and primate COVID-19 risk

Amanda D. Melin; Mareike C. Janiak; Frank Marrone; Paramjit S. Arora; James P. Higham

. CC-BY-NC-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.09.034967 doi: bioRxiv preprint Table 1 . Results of protein-protein interaction experiments predicting impact of amino acid changes, relative to human ACE2 residues, at critical binding sites with SARS-CoV-2 receptor binding domain. Impacts of changes across the full complement of critical binding sites are presented in (A), single residue replacements are presented in (B). The copyright holder for this preprint (which was not peer-reviewed) is the . Figure 1 . ACE2 protein sequence alignment and phylogeny of study species. Branch lengths represent evolutionary distance estimated from TimeTree.org 27 . We outline amino acid residues at critical binding sites for the SARS-CoV-2 spike receptor binding domain. Solid outlines highlight sites predicted to have the most substantial impact on viral binding affinity. Notably, protein sequences of catarrhine primates are highly conserved, including uniformity among amino acids at all binding sites. Primate species that are able to be successfully infected with COVID-19 are indicated in red. Predicted susceptibility to COVID-19 for other primates is additionally coded by terminal branch colors. The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.09.034967 doi: bioRxiv preprint