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Title: Binding of SARS-COV-2 (COVID-19) and SARS-COV to human ACE2: Identifying binding sites and consequences on ACE2 stiffness
Award ID(s):
2019077
PAR ID:
10297618
Author(s) / Creator(s):
; ;
Date Published:
Journal Name:
Chemical Physics
Volume:
551
Issue:
C
ISSN:
0301-0104
Page Range / eLocation ID:
111353
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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  1. We report a distinct difference in the interactions of the glycans of the host-cell receptor, ACE2, with SARS-CoV-2 and SARS-CoV S–protein receptor-binding domains (RBDs). Our analysis demonstrates that the ACE2 glycan at N322 enhances interactions with the SARS-CoV-2 RBD while the ACE2 glycan at N90 may offer protection against infections of both coronaviruses depending on its composition. The interactions of the ACE2 glycan at N322 with SARS-CoV RBD are blocked by the presence of the RBD glycan at N357 of the SARS-CoV RBD. The absence of this glycosylation site on SARS-CoV-2 RBD may enhance its binding with ACE2. 
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