RT Journal Article
SR Electronic
T1 N and O glycosylation of the SARS-CoV-2 spike protein
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.07.05.187344
DO 10.1101/2020.07.05.187344
A1 Miloslav Sanda
A1 Lindsay Morrison
A1 Radoslav Goldman
YR 2020
UL http://biorxiv.org/content/early/2020/07/06/2020.07.05.187344.abstract
AB Covid-19 pandemic outbreak is the reason of the current world health crisis. The development of effective antiviral compounds and vaccines requires detailed descriptive studies of the SARS-CoV-2 proteins. The SARS-CoV-2 spike (S) protein mediates virion binding to the human cells through its interaction with the ACE2 cell surface receptor and is one of the prime immunization targets. A functional virion is composed of three S1 and three S2 subunits created by furin cleavage of the spike protein at R682, a polybasic cleavage sites that differs from the SARS-CoV spike protein of 2002. We observe that the spike protein is O-glycosylated on a threonine (T678) near the furin cleavage site occupied by core-1 and core-2 structures. In addition, we have identified eight additional O-glycopeptides on the spike glycoprotein and we confirmed that the spike protein is heavily N-glycosylated. Our recently developed LC-MS/MS methodology allowed us to identify LacdiNAc structural motifs on all occupied N-glycopeptides and polyLacNAc structures on six glycopeptides of the spike protein. In conclusion, our study substantially expands the current knowledge of the spike protein’s glycosylation and enables the investigation of the influence of the O-glycosylation on its proteolytic activation.Competing Interest StatementThe authors have declared no competing interest.