SARS-CoV-2 Glycosylation

SARS-CoV-2 glycosylation is at the forefront of today’s corona virus research. 

The SARS-CoV-2 corona virus outer surface is coated with spike proteins. The viruses spike protein binds to the ACE2 receptor mediating cell entry and membrane fusion. Both are highly glycosylated. From 55-74 N-linked glycans and at least 2 O-linked glycans encapsulate each protein in a glycan shield.

The spike protein is the primary antigen in the development of vaccines against this virus. The glycosylation of the recombinant proteins and glycopeptides being developed as antigens are critical to their function and success. The heterogeneity of these glycans under different culture conditions may have an impact on the antigenicity of the spike glycoprotein.

Our partners at Ludger Ltd (Oxford, UK) are offering glycoanalytical services for SARS-CoV-2 samples. They have over twenty years of experience analysing glycosylation and are well regarded in the glycobiology community. 

Please contact us for further details.

Corona virus image

Sample types:

  • COVID-19 patient samples (e.g. plasma, tissues)
  • SARS-CoV-2 infected cell lines
  • Vaccine candidates
  • mAbs, glycoprotein hormones, Fc fusion proteins

Services available:

  • Glycosylation Site Analysis
  • Detailed Glycan Characterisation
  • Glycan Profiling Analysis
  • Glycan Antennary Profiling Analysis

SARS-CoV-2 / ACE2 Glycosylation References

– Celia Henry Arnaud. Adding the missing sugars to coronavirus protein structures Chemical and Engineering News 98: 16 (22 April 2020)

– Asif Shajahan, Nitin T. Supekar, Anne S. Gleinich, Parastoo Azadi. Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2 Glycobiology doi: 10.1093/glycob/cwaa042 (6 April 2020)

– Oliver C. Grant, David Montgomery, Keigo Ito, and Robert J. Woods Analysis of the SARS-CoV-2 spike protein glycan shield: implications for immune recognition Preprint (1 May 2020)

– Asif Shajahan, Stephanie Archer-Hartmann, Nitin T. Supekar, Anne S. Gleinich, Christian Heiss, Parastoo Azadi Comprehensive characterization of N- and O- glycosylation of SARS-CoV-2 human receptor angiotensin converting enzyme 2 Glycobiology doi: 10.1093/glycob/cwaa101 (2 May 2020)

– Yasunori Watanabe, Zachary T. Berndsen, Jayna Raghwani, Gemma E. Seabright, Joel D. Allen, Oliver G. Pybus, Jason S. McLellan, Ian A. Wilson, Thomas A. Bowden, Andrew B. Ward & Max Crispin. Vulnerabilities in coronavirus glycan shields despite extensive glycosylation Nature Communications 11, Article number: 2688 (27 May 2020)

– Yong Zhang, Wanjun Zhao, Yonghong Mao, Yaohui Chen, Shisheng Wang, Yi Zhong, Tao Su, Meng Gong, Dan Du, Xiaofeng Lu, Jingqiu Cheng, Hao Yang. Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins Molecular & Cellular Proteomics doi: 10.1074/mcp.ra120.002295 (30 June 2020)

– Miloslav Sanda, Lindsay Morrison, Radoslav Goldman. N and O glycosylation of the SARS-CoV-2 spike protein Analytical Chemistry doi: 10.1021/acs.analchem.0c03173 (6 July 2020)

– Yasunori Watanabe, Joel D. Allen, Daniel Wrapp, Jason S. McLellan, Max Crispin. Site-specific glycan analysis of the SARS-CoV-2 spike Science : Vol. 369, Issue 6501, pp. 330-333, (17 Jul 2020)

– Wenxin Xu, Mingjie Wang Demin Yu, Xinxin Zhang. Variations in SARS-CoV-2 Spike Protein Cell Epitopes and Glycosylation Profiles During Global Transmission Course of COVID-19 Front. Immunol., 4 September 2020

– Oliver C. Grant, David Montgomery, Keigo Ito & Robert J. Woods. Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition Scientific Reports 10, Article number: 14991 (14 September 2020)

– Peng Zhao, Jeremy L. Praissman, Oliver C. Grant, Yongfei Cai, Tianshu Xiao, Katelyn E. Rosenbalm, Kazuhiro Aoki, Benjamin P. Kellman, Robert Bridger, Dan H. Barouch, Melinda A. Brindley, Nathan E. Lewis, Michael Tiemeyer, Bing Chen, Robert J. Woods, and Lance Wells Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor Cell Host Microbe. 28(4): 586–601.e6. (7 October 2020)