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 journalArticlepeer-review

20 Scopus citations


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 languageEnglish (US)
Pages (from-to)5949-5952
Number of pages4
JournalChemical Communications
Issue number48
StatePublished - Jun 18 2021
Externally publishedYes

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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