Issue 48, 2021
From the journal:

Chemical Communications

ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV†

Atanu Acharya, ORCID logo *a   Diane L. Lynch,a   Anna Pavlova,a   Yui Tik Pang ORCID logo a  and  James C. Gumbart ORCID logo *a  

* Corresponding authors

a School of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA
E-mail: aacharya42@gatech.edu, gumbart@physics.gatech.edu

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.

Graphical abstract: ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV

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Article information

DOI
https://doi.org/10.1039/D1CC02305E
Article type
Communication
Submitted
30 Apr 2021
Accepted
18 May 2021
First published
18 May 2021

Chem. Commun., 2021,57, 5949-5952

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ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV

A. Acharya, D. L. Lynch, A. Pavlova, Y. T. Pang and J. C. Gumbart, Chem. Commun., 2021, 57, 5949 DOI: 10.1039/D1CC02305E

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