Author: Asif Shajahan; Nitin T. Supekar; Anne S. Gleinich; Parastoo Azadi
Title: Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2 Document date: 2020_4_3
ID: f0xsisdg_17
Snippet: We discovered predominantly highly processed sialylated complex-type glycans on sites N165, N282, N801, and N1098 ( Similar to one recent report, we observed Man5GlcNAc2 as a predominant structure across all sites (Watanabe, Y., Allen, J.D., et al. 2020 ). However, we observed significantly unoccupied peptides on both S1 and S2 subunits. Sites N17, N603, N1134, N1158 and N1173 were completely unoccupied, although further studies with higher conce.....
Document: We discovered predominantly highly processed sialylated complex-type glycans on sites N165, N282, N801, and N1098 ( Similar to one recent report, we observed Man5GlcNAc2 as a predominant structure across all sites (Watanabe, Y., Allen, J.D., et al. 2020 ). However, we observed significantly unoccupied peptides on both S1 and S2 subunits. Sites N17, N603, N1134, N1158 and N1173 were completely unoccupied, although further studies with higher concentration and purity of proteins are required to validate this finding (Figure 1 , 2). On subunit S2, the detection of N-glycosylation at sites N709, N717, and N1134 was ambiguous as the quality of the MS/MS spectra was not satisfactory and we are currently evaluating the possibilities of other post translational modifications adjacent to these sites.
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