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dc.contributor.authorSynowsky, Silvia A.
dc.contributor.authorShirran, Sally L.
dc.contributor.authorCooke, Fiona G. M.
dc.contributor.authorAntoniou, Antony N.
dc.contributor.authorBotting, Catherine H.
dc.contributor.authorPowis, Simon J.
dc.date.accessioned2017-09-01T11:30:11Z
dc.date.available2017-09-01T11:30:11Z
dc.date.issued2017-10-13
dc.identifier.citationSynowsky , S A , Shirran , S L , Cooke , F G M , Antoniou , A N , Botting , C H & Powis , S J 2017 , ' The major histocompatibility complex class I immunopeptidome of extracellular vesicles ' Journal of Biological Chemistry , vol. 292 , pp. 17084-17092 . https://doi.org/10.1074/jbc.M117.805895en
dc.identifier.issn0021-9258
dc.identifier.otherPURE: 250989908
dc.identifier.otherPURE UUID: d085c318-391b-4a38-8606-7297c2728cf2
dc.identifier.otherScopus: 85031329578
dc.identifier.otherORCID: /0000-0003-3516-3507/work/36476312
dc.identifier.urihttp://hdl.handle.net/10023/11593
dc.descriptionThis work was funded by the Melville Trust for the Care and Cure of Cancer, Scotland, UK.en
dc.description.abstractExtracellular vesicles (EVs) are released by most cell types and have been associated with multiple immunomodulatory functions. MHC class I molecules have crucial roles in antigen presentation and in eliciting immune responses and are known to be incorporated into EVs. However, the MHC class Iimmunopeptidome of EVs has not been established. Here, using a small-scale immunoisolation of the antigen serotypes HLA-A*02:01 and HLA-B*27:05 expressed on the Epstein–Barr virus–transformed B cell line Jesthom and MS of the eluted peptides from both cells and EVs, we identified 516 peptides that bind either HLA-A*02:01 orHLA-B*27:05. Of importance, the predicted serotype-binding affinities and peptide-anchor motifs did not significantly differ between the peptide pools isolated from cells or EVs,indicating that during EV biogenesis, no obvious editing of the MHC class Iimmunopeptidome occurs. These results, for the first time, establish EVs as a source ofMHC class I peptides that can be used for the study of the immunopeptidome and in the discovery of potential neoantigens for immunotherapies.en
dc.language.isoeng
dc.relation.ispartofJournal of Biological Chemistryen
dc.rights© 2017, American Society for Biochemistry and Molecular Biology, Inc. This work has been made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at www.jbc.org / https://doi.org/10.1074/jbc.M117.805895en
dc.subjectExtracellular vesiclesen
dc.subjectimmunologyen
dc.subjectMajor Histocompatibility Complexen
dc.subjectMass spectrometryen
dc.subjectProteomicsen
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectQR180 Immunologyen
dc.subjectRM Therapeutics. Pharmacologyen
dc.subjectDASen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.subject.lccQR180en
dc.subject.lccRMen
dc.titleThe major histocompatibility complex class I immunopeptidome of extracellular vesiclesen
dc.typeJournal articleen
dc.description.versionPostprinten
dc.description.versionPostprinten
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. School of Medicineen
dc.contributor.institutionUniversity of St Andrews. Cellular Medicine Divisionen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1074/jbc.M117.805895
dc.description.statusPeer revieweden


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