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http://purl.uniprot.org/citations/37471227http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37471227http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37471227http://www.w3.org/2000/01/rdf-schema#comment"CD4+ T cells recognize a broad range of peptide epitopes of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which contribute to immune memory and limit COVID-19 disease. We demonstrate that the immunogenicity of SARS-CoV-2 peptides, in the context of the model allotype HLA-DR1, does not correlate with their binding affinity to the HLA heterodimer. Analyzing six epitopes, some with very low binding affinity, we solve X-ray crystallographic structures of each bound to HLA-DR1. Further structural definitions reveal the precise molecular impact of viral variant mutations on epitope presentation. Omicron escaped ancestral SARS-CoV-2 immunity to two epitopes through two distinct mechanisms: (1) mutations to TCR-facing epitope positions and (2) a mechanism whereby a single amino acid substitution caused a register shift within the HLA binding groove, completely altering the peptide-HLA structure. This HLA-II-specific paradigm of immune escape highlights how CD4+ T cell memory is finely poised at the level of peptide-HLA-II presentation."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2023.112827"xsd:string
http://purl.uniprot.org/citations/37471227http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2023.112827"xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Sewell A.K."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Sewell A.K."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Rizkallah P."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Rizkallah P."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Godkin A."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Godkin A."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Gallimore A.M."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Gallimore A.M."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Greenshields-Watson A."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Greenshields-Watson A."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Long H.M."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Long H.M."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"MacLachlan B.J."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"MacLachlan B.J."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Mason G.H."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Mason G.H."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Haigh T.A."xsd:string
http://purl.uniprot.org/citations/37471227http://purl.uniprot.org/core/author"Haigh T.A."xsd:string