Author: Yasunori Watanabe; Zachary T. Berndsen; Jayna Raghwani; Gemma E. Seabright; Joel D. Allen; Jason S. McLellan; Ian A. Wilson; Thomas A. Bowden; Andrew B. Ward; Max Crispin
Title: Vulnerabilities in coronavirus glycan shields despite extensive glycosylation Document date: 2020_2_21
ID: bnnt05fn_23
Snippet: For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan "shield" over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosyla.....
Document: For example, both LASV GPC and coronavirus S proteins consist of 25% glycan by molecular weight. However, given the significantly larger protein surface area and volume of coronavirus S proteins, coverage of the glycan "shield" over the proteinaceous surface is considerably sparser in comparison to the smaller LASV GPC, which occludes a far greater proportion of the protein surface with fewer glycans. To demonstrate that the presence of glycosylation plays a major role in the immune response to these different glycoproteins, we studied the glycome of several biomedically important coronaviruses and compared their glycan compositions in a structural context.
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