Site-specific analysis of the SARS-CoV-2 glycan shield

Yasunori Watanabe; Joel D. Allen; Daniel Wrapp; Jason S. McLellan; Max Crispin

. CC-BY 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.26.010322 doi: bioRxiv preprint The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.26.010322 doi: bioRxiv preprint fragmentation, and the glycan compositions at each site were determined for all 22 N-linked glycan sites on the SARS-CoV-2 S protein (Figure 2) . A diverse range of glycan compositions were observed across the different glycosylation sites. In order to convey the main processing features at each site, the abundances of each glycan are summed into oligomannose-, hybridand complex-type glycosylation. In addition, the diverse signals arising from heterogeneous complex-type glycosylation are simplified by the summation of glycan intensities into a more limited range of structural categories.