Author: Joana Damas; Graham M. Hughes; Kathleen C. Keough; Corrie A. Painter; Nicole S. Persky; Marco Corbo; Michael Hiller; Klaus-Peter Koepfli; Andreas R. Pfenning; Huabin Zhao; Diane P. Genereux; Ross Swofford; Katherine S. Pollard; Oliver A. Ryder; Martin T. Nweeia; Kerstin Lindblad-Toh; Emma C. Teeling; Elinor K. Karlsson; Harris A. Lewin
Title: Broad Host Range of SARS-CoV-2 Predicted by Comparative and Structural Analysis of ACE2 in Vertebrates Document date: 2020_4_18
ID: 6ne76rh1_7
Snippet: Site-directed mutagenesis and co-precipitation of SARS-CoV constructs have revealed critical residues on the ACE2 tertiary structure that are essential for binding to the virus receptor binding domain (RBD) (19) . These findings have been strongly supported by co-crystallization and the structural determination of the SARS-CoV and SARS-CoV-2 S proteins with human ACE2 (13, 20, 21) , as well as binding-affinity with heterologous ACE2 (19) . The RB.....
Document: Site-directed mutagenesis and co-precipitation of SARS-CoV constructs have revealed critical residues on the ACE2 tertiary structure that are essential for binding to the virus receptor binding domain (RBD) (19) . These findings have been strongly supported by co-crystallization and the structural determination of the SARS-CoV and SARS-CoV-2 S proteins with human ACE2 (13, 20, 21) , as well as binding-affinity with heterologous ACE2 (19) . The RBD of human coronaviruses may mutate to change the binding affinity of S for ACE2, and thus lead to adaptation in humans or other hosts. The best studied example is the palm civet, believed to have been the intermediate host between bats and humans for SARS-CoV (2) .
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