We discovered predominantly highly processed sialylated complex-type glycans on sites N165, N282, N801, N1074 and N1098 and.
Sites N17, N603, N1134, N1158 and N1173 were completely unoccupied, although further studies with higher concentration, alternative protease digestion strategies and purity of proteins are required to validate this finding and.
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Possibly, Ser325 is occupied with HexNAcHexNeuAc glycan together with T323 , but this could not be confirmed unambiguously as electron transfer dissociation fragmentation on this peptide was not successful because of lower charge states of peptide Supplementary and.
We used recombinant SARS-CoV-2 subunit S1 and S2 expressed in human cells, HEK 293, and observed partial N-glycan occupancy on 17 out of 22 N-glycosylation sites.
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Interestingly, our O-glycoproteomic profiling indicated O-glycosylation at sites Thr323 and Ser325 on the S1 subunit of SARS-CoV-2 spike protein , and.