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N and O glycosylation of the SARS-CoV-2 spike protein

View ORCID ProfileMiloslav Sanda, Lindsay Morrison, Radoslav Goldman
doi: https://doi.org/10.1101/2020.07.05.187344
Miloslav Sanda
1Georgetown University, Department of Oncology, 3800 Reservoir Rd NW, Washington, D.C. 20057
3Georgetown University, Clinical and Translational Glycoscience Research Center, 3800 Reservoir Rd NW, Washington, D.C. 20057
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  • For correspondence: ms2465@georgetown.edu
Lindsay Morrison
4Waters Corporation Inc., Beverly, MA 01915 USA
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Radoslav Goldman
1Georgetown University, Department of Oncology, 3800 Reservoir Rd NW, Washington, D.C. 20057
2Georgetown University, Department of Biochemistry and Molecular & Cellular Biology, 3800 Reservoir Rd NW, Washington, D.C. 20057
3Georgetown University, Clinical and Translational Glycoscience Research Center, 3800 Reservoir Rd NW, Washington, D.C. 20057
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Abstract

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 Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted July 06, 2020.
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N and O glycosylation of the SARS-CoV-2 spike protein
Miloslav Sanda, Lindsay Morrison, Radoslav Goldman
bioRxiv 2020.07.05.187344; doi: https://doi.org/10.1101/2020.07.05.187344
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N and O glycosylation of the SARS-CoV-2 spike protein
Miloslav Sanda, Lindsay Morrison, Radoslav Goldman
bioRxiv 2020.07.05.187344; doi: https://doi.org/10.1101/2020.07.05.187344

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