Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2

Asif Shajahan; Nitin T. Supekar; Anne S. Gleinich; Parastoo Azadi

The glycosylation pattern of the spike protein is a crucial characteristic to be considered regarding steric hindrance, chemical properties and even as a potential target for mutation in the future. The N-glycans on S protein play important roles in proper protein folding and priming by host proteases. Since glycans can shield the amino acid residues and other epitopes from cells and antibody recognition, glycosylation can enable the coronavirus to evade both the innate and adaptive immune responses (Walls, A.C., Park, Y.J., et al. 2020 , Walls, A.C., Xiong, X., et al. 2019 . Elucidating the glycosylation of the viral S protein can aid in understanding viral binding with receptors, fusion, entry, replication and also in designing suitable antigens for vaccine development (Chakraborti, S., Prabakaran, P., et al. 2005 , Watanabe, Y., Bowden, T.A., et al. 2019 , Zheng, J., Yamada, Y., et al. 2018 . Strategies for vaccine development aim to elicit such adaptive immunity through an antibody response at the sites of viral entry (Afrough, B., Dowall, S., et al. 2019 ).