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PXD024562

PXD024562 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleDigging deeper into the HLA peptidome – Characterization of the post-translationally modified peptides
DescriptionPeptides displayed by MHC molecules on a cell’s surface, referred to as its immunopeptidome, play an important role in the adaptive the immune response. Antigen processing for MHC class I presentation is a ubiquitous pathway present in all nucleated cells which generate and present peptides of both self and non-self origin. Peptides with post-translational modifications (PTMs) are one of the classes of peptides presented by MHC class I molecules. However, due to the high background of self-peptides presented by the cells, the diversity of peptides with post-translational modifications is not well reported. In this study, we have carried out MHC Class I immunopeptidomics analysis on Jurkat and A375 cell lines to characterize the diversity of post-translational modifications among MHC class I peptides. Using high resolution mass spectrometry, we identified 25,761 MHC-bound peptides across both the cell lines using Bolt and Sequest search engines. High specificity of the enrichment method is demonstrated by identifying ~90% of the peptides with typical length distribution of 8-12 aa and enriched motifs within those peptides similar to the binding motifs of MHC alleles. Among the MHC-bound peptides, we identified phosphorylation as a major post-translational modification followed by deamidation. We observed site-specific localization of these post-translational modifications, at position P4 for phosphorylated peptides and position P3 for deamidated peptides. We identified a smaller number of peptides with acetylated and methylated lysine, possibly due to very low stoichiometric levels of these post-translational modifications compared to phosphorylation and deamidation. Using PEAKS de novo sequencing algorithm, we identified spliced peptides that account for ~5-7% of MHC-bound peptides across the two cell lines. These peptides share similar features with respect to normal MHC-bound peptides such as peptide length distribution and binding motifs. We validated the identification of several post-translationally modified peptides and spliced peptides using synthetic peptide sequences. In conclusion, our study demonstrates unbiased identification of these low stoichiometric PTMs and unusual spliced peptides using high resolution mass spectrometry.
HostingRepositoryPRIDE
AnnounceDate2021-06-07
AnnouncementXMLSubmission_2021-06-07_08:18:48.006.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAkhilesh Pandey
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue; deamidated residue
InstrumentOrbitrap Eclipse
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-03-07 23:25:50ID requested
12021-06-07 08:18:48announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Immunopeptidome, MHC class I, MHC binding motifs, Post-translational modifications, Spliced peptides
Contact List
Akhilesh Pandey
contact affiliationDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN 55905, USA Center for Individualized Medicine, Mayo Clinic, Rochester, MN 55905, USA
contact emailPandey.Akhilesh@mayo.edu
lab head
Akhilesh Pandey
contact affiliationDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN 55905
contact emailpandey.akhilesh@mayo.edu
dataset submitter
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