Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.09.12.294504v1?rss=1 Authors: Rahnama, S., Azimzadeh Irani, M., Amininasab, M., Ejtehadi, R. Abstract: SARS-COV-2 is a strain of Coronavirus family which caused the extensive pandemic of COVID-19, which is still going on. Several studies showed that the glycosylation of virus spike (S) protein and the Angiotensin-Converting Enzyme 2 (ACE2) receptor on the host cell is critical for the virus infectivity. Molecular Dynamics (MD) simulations were used to explore the role of a novel mutated O-glycosylation site (D494S) on the Receptor Binding Domain (RBD) of S protein. This site was suggested as a key mediator of virus-host interaction. We showed that the decoration of S494 with core and elongated O-glycans results in stabilized interactions on the direct RBD-ACE2 interface with more favorable binding free energies for longer oligosaccharides. Hence, the further drug design attempts should take this crucial factor into account, while suggesting any novel therapeutic candidate. Copy rights belong to original authors. Visit the link for more info