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_12
Snippet: Given that the receptor binding domain is the main target of neutralising antibodies 12 The copyright holder for this preprint (which was not peer-reviewed) is the .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 The modelling of the experimentally observed glycosylation is illustrated on the pre-fusion structure of trimeric MERS S (PDB ID 5X59) 17 and SARS S (PDB ID 5X58) 17 glycoproteins. The glycans are colored according to ol.....
Document: Given that the receptor binding domain is the main target of neutralising antibodies 12 The copyright holder for this preprint (which was not peer-reviewed) is the .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 The modelling of the experimentally observed glycosylation is illustrated on the pre-fusion structure of trimeric MERS S (PDB ID 5X59) 17 and SARS S (PDB ID 5X58) 17 glycoproteins. The glycans are colored according to oligomannose content, as defined by the key. DPP4 receptor binding sites and ACE2 receptor binding sites for MERS and SARS, respectively, are indicated in light blue. The S1 and S2 subunits are colored light grey and dark grey, respectively.
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