Author: Yasunori Watanabe; Joel D. Allen; Daniel Wrapp; Jason S. McLellan; Max Crispin
Title: Site-specific analysis of the SARS-CoV-2 glycan shield Document date: 2020_3_28
ID: 63j4qc7d_9
Snippet: There are three sites on SARS-CoV-2 that are predominantly oligomannose-type: N234, N709 and N801. The predominant structure observed at each site, with the exception of N234, is Man5GlcNAc2, which demonstrates that these sites are largely accessible to a ï¡1,2mannosidases but are poor substrates for GlcNAcT-I, which is the gateway enzyme in the formation of hybrid-and complex-type glycans in the Golgi apparatus. The stage at which processing is.....
Document: There are three sites on SARS-CoV-2 that are predominantly oligomannose-type: N234, N709 and N801. The predominant structure observed at each site, with the exception of N234, is Man5GlcNAc2, which demonstrates that these sites are largely accessible to a ï¡1,2mannosidases but are poor substrates for GlcNAcT-I, which is the gateway enzyme in the formation of hybrid-and complex-type glycans in the Golgi apparatus. The stage at which processing is impeded is a signature related to the density and presentation of glycans on the viral spike. For example, the more densely glycosylated spikes of HIV-1 Env and Lassa virus GPC give rise to numerous sites dominated by Man9GlcNAc2 [20] [21] [22] 26 .
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