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Title: ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV
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.  more » « less
Award ID(s):
1828187
PAR ID:
10318230
Author(s) / Creator(s):
; ; ; ;
Date Published:
Journal Name:
Chemical Communications
Volume:
57
Issue:
48
ISSN:
1359-7345
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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