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

Atanu Acharya; Diane L. Lynch; Anna Pavlova; Yui Tik Pang; James C. Gumbart

doi:10.1039/d1cc02305e

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

Atanu Acharya, Diane L. Lynch, Anna Pavlova, Yui Tik Pang, James C. Gumbart

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

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.

Original language	English (US)
Pages (from-to)	5949-5952
Number of pages	4
Journal	Chemical Communications
Volume	57
Issue number	48
DOIs	https://doi.org/10.1039/d1cc02305e
State	Published - Jun 18 2021
Externally published	Yes

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
General Chemistry
Ceramics and Composites
Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Catalysis

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title = "ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV",

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.",

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T1 - ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV

AU - Acharya, Atanu

AU - Lynch, Diane L.

AU - Pavlova, Anna

AU - Pang, Yui Tik

AU - Gumbart, James C.

PY - 2021/6/18

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

Abstract

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