Fine-tuning the spike: role of the nature and topology of the glycan shield in the structure and dynamics of the SARS-CoV-2 S
Aoife M. Harbison, Carl A. Fogarty, Toan K. Phung, Akash Satheesan, Benjamin L. Schulz, Elisa Fadda
Abstract
-glycosylation at N370 stabilizes the closed RBD conformation by binding a specific cleft on the RBD surface. We discuss how the absence of the N370 glycan in the SARS-CoV-2 S frees the RBD glycan binding cleft, which becomes available to bind cell-surface glycans, and potentially increases host cell surface localization.
Topics & Concepts
GlycanGlycosylationEctodomainMolecular dynamicsInfectivityN-linked glycosylationTopology (electrical circuits)Cell biologyBiologyBiophysicsChemistryGlycoproteinReceptorVirologyBiochemistryVirusComputational chemistryMathematicsCombinatoricsSARS-CoV-2 and COVID-19 ResearchInfluenza Virus Research StudiesViral Infections and Outbreaks Research