Glycans Modulate the Adsorption of RBD Glycoproteins on Polarizable Surfaces.

Area of Science:

• Biophysics
• Surface Science
• Virology

Background:

• Respiratory viruses spread via airborne droplets that can land on surfaces (fomites).
• The interaction of viral glycoproteins with surfaces is crucial for transmission but not fully understood.
• Glycans, sugar molecules on proteins, may act as key modulators of these interactions.

Purpose of the Study:

• To investigate the role of glycans in the adsorption of SARS-CoV-2 Receptor Binding Domain (RBD) to polarizable surfaces.
• To understand how glycan location and protein conformation affect adsorption mechanisms.
• To explore the potential of glycans as modulators of viral glycoprotein-surface interactions.

Main Methods:

• Molecular dynamics simulations were used to model the adsorption of SARS-CoV-2 RBD variants.
• Simulations focused on interactions with both hydrophobic and hydrophilic polarizable planar interfaces.
• Analysis examined the influence of glycan position, protein conformation (open/closed), and mutations (Omicron) on adsorption.

Main Results:

• Hydrophobic surfaces promoted stable adsorption for both open and closed RBD conformations.
• Hydrophilic surfaces showed reduced adsorption, especially for the closed RBD, with glycans forming hydrogen bonds.
• Glycans significantly altered closed RBD adsorption, either stabilizing or hindering it based on conformation, mutations, and initial glycan placement.

Conclusions:

• Glycans play a critical role in modulating glycoprotein adsorption to surfaces, impacting viral behavior.
• Findings provide fundamental insights into glycan-protein-surface interactions relevant to virus transmission and fomite dynamics.
• This research opens avenues for understanding glycan roles in protein aggregation and biological recognition at interfaces.