tetano
Editor, Senior Moderator
Chem Commun (Camb)
. 2021 May 21.
doi: 10.1039/d1cc02305e. Online ahead of print.
ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV
Atanu Acharya[SUP] 1 [/SUP], Diane L Lynch[SUP] 1 [/SUP], Anna Pavlova[SUP] 1 [/SUP], Yui Tik Pang[SUP] 1 [/SUP], James C Gumbart[SUP] 1 [/SUP]
Affiliations
Abstract
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.
. 2021 May 21.
doi: 10.1039/d1cc02305e. Online ahead of print.
ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV
Atanu Acharya[SUP] 1 [/SUP], Diane L Lynch[SUP] 1 [/SUP], Anna Pavlova[SUP] 1 [/SUP], Yui Tik Pang[SUP] 1 [/SUP], James C Gumbart[SUP] 1 [/SUP]
Affiliations
- PMID: 34019602
- DOI: 10.1039/d1cc02305e
Abstract
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.