ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV
Atanu Acharya, Diane L. Lynch, Ànna Pavlova, Yui Tik Pang, James C. Gumbart
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.
Topics & Concepts
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)GlycanCoronavirus disease 2019 (COVID-19)2019-20 coronavirus outbreakVirologyChemistrySars virusBetacoronavirusComputational biologyBiologyMedicineBiochemistryGlycoproteinOutbreakPathologyDiseaseInfectious disease (medical specialty)SARS-CoV-2 and COVID-19 ResearchCOVID-19 Clinical Research StudiesAnimal Virus Infections Studies