Since its emergence in 2019, the SARS-CoV-2 coronavirus has led to a public health crisis impacting the lives of people worldwide. The development of treatments to combat COVID-19 (the disease caused by SARS-Cov-2) requires an understanding of the structure and function of different components of the virus. For example, SARS-CoV-2 has spike proteins on its surface that enable the virus to invade human cells and cause infection. The spike proteins of SARS-CoV-2 are covered in sugar molecules called glycans that impact how the virus functions. Though research has revealed a lot about the functions of spike proteins, extensive knowledge of how glycans are arranged on spike proteins is needed to provide new insights into how SARS-Cov-2 functions and how it can be treated.

The goal of the Common Fund’s Glycoscience program is to develop resources that make the study of glycans more accessible to the research community. In research supported by the Common Fund, Dr. Radoslav Goldman and colleagues developed methods to quantify the different glycan structures attached to specific positions on proteins. The researchers then applied these methods to develop a nuanced, in-depth portrait of the structure of glycans on SARS-CoV-2 spike proteins. By analyzing spike proteins expressed in lab-grown human cells, the researchers identified eight novel glycopeptides (peptides with glycans attached to them), showing the specific locations of the sugars on SARS-CoV-2 spike proteins in great detail. This work considerably expands knowledge of the structure of SARS-CoV-2, paving the way for deeper insights into how glycans impact virus function.

References

• Low Collision Energy Fragmentation in Structure-Specific Glycoproteomics Analysis. Miloslav Sanda, Julius Benicky, Radoslav Goldman. Anal Chem. 2020 Jun 16; 92(12):8262-8267.
• N- and O-Glycosylation of the SARS-CoV-2 Spike Protein. Miloslav Sanda, Lindsay Morrison, Radoslav Goldman. Anal Chem. 2021 Feb 2; 93(4):2003-2009.