{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(12)"],"submitter":["Hafstrand I"],"funding":["Vetenskapsrådet","Cancerfonden"],"pubmed_abstract":["Post-translational modifications significantly broaden the epitope repertoire for major histocompatibility class I complexes (MHC-I) and may allow viruses to escape immune recognition. Lymphocytic choriomeningitis virus (LCMV) infection of H-2b mice generates CD8+ CTL responses directed towards several MHC-I-restricted epitopes including the peptides GP92 (CSANNSHHYI) and GP392 (WLVTNGSYL), both with a N-glycosylation site. Interestingly, glycosylation has different effects on the immunogenicity and association capacity of these two epitopes to H-2Db. To assess the structural bases underlying these functional results, we determined the crystal structures of H-2Db in complex with GP92 (CSANNSHHYI) and GP392 (WLVTNGSYL) to 2.4 and 2.5 Å resolution, respectively. The structures reveal that wh"],"journal":["PloS one"],"pagination":["e0189584"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5734757"],"repository":["biostudies-literature"],"pubmed_title":["Crystal structures of H-2Db in complex with the LCMV-derived peptides GP92 and GP392 explain pleiotropic effects of glycosylation on antigen presentation and immunogenicity."],"pmcid":["PMC5734757"],"pubmed_authors":["Norstrom M","Buratto J","Duru AD","Pellegrino S","Achour A","Josey BJ","Hafstrand I","Sandalova T","Badia-Martinez D"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structures of H-2Db in complex with the LCMV-derived peptides GP92 and GP392 explain pleiotropic effects of glycosylation on antigen presentation and immunogenicity.","description":"Post-translational modifications significantly broaden the epitope repertoire for major histocompatibility class I complexes (MHC-I) and may allow viruses to escape immune recognition. Lymphocytic choriomeningitis virus (LCMV) infection of H-2b mice generates CD8+ CTL responses directed towards several MHC-I-restricted epitopes including the peptides GP92 (CSANNSHHYI) and GP392 (WLVTNGSYL), both with a N-glycosylation site. Interestingly, glycosylation has different effects on the immunogenicity and association capacity of these two epitopes to H-2Db. To assess the structural bases underlying these functional results, we determined the crystal structures of H-2Db in complex with GP92 (CSANNSHHYI) and GP392 (WLVTNGSYL) to 2.4 and 2.5 Å resolution, respectively. The structures reveal that wh","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017","modification":"2026-04-07T15:51:04.994Z","creation":"2019-03-27T03:05:06Z"},"accession":"S-EPMC5734757","cross_references":{"pubmed":["29253009"],"doi":["10.1371/journal.pone.0189584"]}}