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dc.creatorGrant, Oliver C.
dc.creatorMontgomery, David
dc.creatorIto, Keigo
dc.creatorWoods, Robert J.
dc.date.accessioned2020-09-17T17:16:04Z
dc.date.available2020-09-17T17:16:04Z
dc.date.created2020
dc.identifier.issn2045 2322spa
dc.identifier.otherhttps://doi.org/10.1038/s41598-020-71748-7spa
dc.identifier.urihttp://hdl.handle.net/20.500.12010/13372
dc.description.abstractHere we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those present in the nascent glycoproteins (prior to enzymatic modifcations in the Golgi), as well as those that are commonly observed on antigens present in other viruses. These models were subjected to molecular dynamics (MD) simulation to determine the extent to which glycan microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we have identifed peptides in the S glycoprotein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the innate and adaptive immune response to the SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specifc glycoform. Despite the relatively modest contribution of the glycans to the total molecular weight of the S trimer (17% for the HEK293 glycoform) they shield approximately 40% of the protein surface.spa
dc.format.extent11 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.language.isoengspa
dc.publisherScientific reportsspa
dc.sourcereponame:Expeditio Repositorio Institucional UJTLspa
dc.sourceinstname:Universidad de Bogotá Jorge Tadeo Lozanospa
dc.subjectAnalysis of the SARS‑CoV‑2spa
dc.subjectSpike protein glycanspa
dc.subjectImmune recognitionspa
dc.titleAnalysis of the SARS‑CoV‑2 spike protein glycan shield reveals implications for immune recognitionspa
dc.type.localArtículospa
dc.subject.lembSíndrome respiratorio agudo gravespa
dc.subject.lembCOVID-19spa
dc.subject.lembSARS-CoV-2spa
dc.subject.lembCoronavirusspa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.type.hasversioninfo:eu-repo/semantics/acceptedVersionspa
dc.rights.localAbierto (Texto Completo)spa
dc.identifier.doihttps://doi.org/10.1038/s41598-020-71748-7spa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa


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