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N- and O-Glycosylation of the SARS-CoV-2 Spike Protein

  • Miloslav Sanda*
    Miloslav Sanda
    Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, District of Columbia 20057, United States
    Clinical and Translational Glycoscience Research Center, Georgetown University, Washington, District of Columbia 20057, United States
    *Email: [email protected]. Phone: +1 202-6876279. Fax: +1 202-6871988.
    More by Miloslav Sanda
    Orcidhttp://orcid.org/0000-0002-7735-3635
  • , 
  • Lindsay Morrison
    Lindsay Morrison
    Waters Corporation Inc., Beverly, Massachusetts 01915, United States
    More by Lindsay Morrison
  • , and 
  • Radoslav Goldman
    Radoslav Goldman
    Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, District of Columbia 20057, United States
    Department of Biochemistry and Molecular & Cellular Biology, Georgetown University Washington, District of Columbia 20057, United States
    Clinical and Translational Glycoscience Research Center, Georgetown University, Washington, District of Columbia 20057, United States
    More by Radoslav Goldman
    Orcidhttp://orcid.org/0000-0003-1304-0522
Cite this: Anal. Chem. 2021, 93, 4, 2003–2009
Publication Date (Web):January 6, 2021
https://doi.org/10.1021/acs.analchem.0c03173
Copyright © 2021 American Chemical Society
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    Abstract

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    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 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 site that differs from the SARS-CoV spike protein of 2002. By analysis of the protein produced in HEK293 cells, we observe that the spike 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 confirmed that the spike protein is heavily N-glycosylated. Our recently developed liquid chromatography–mass spectrometry 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 O-glycosylation on its proteolytic activation.

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.analchem.0c03173.

    • MS2 spectra of YFKNHTSPDVD O-glycopeptide, cIMS analysis of 657 derived from different T678 O-glycopeptides, HCD spectra of Tn-antigen-occupied T678 O-glycopeptide, and certificate of analysis of SARS-Cov-2 S protein (R683A and R685A), His-tag (PDF)

    • Summary of SARS Cov2 spike glycoprotein glycosylation (XLSX)

    • Data are available in the following link: https://repository.jpostdb.org/preview/14997783515fb8a577b126f, access code: 6639.

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