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_29
Snippet: Overall, this study reveals how the extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, which is reflected by the overall structure, density and oligomannose abundances across the trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vu.....
Document: Overall, this study reveals how the extensive N-linked glycan modifications of SARS and MERS CoV S proteins do not constitute an effective shield, which is reflected by the overall structure, density and oligomannose abundances across the trimeric glycoproteins. We also demonstrate that amino-acid diversification indeed occurs at antibody accessible regions on the trimer, which confirms that glycans play a role in occluding specific regions if vulnerability on the glycoprotein. Furthermore, comparisons between glycan shields from a . 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 It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the .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/10.1101/2020.02.20.957472 doi: bioRxiv preprint number of viruses highlight the importance of a glycan shield in immune evasion and reveal structural principles that govern glycosylation status.
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