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
- 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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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
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