Detection of an HLA-A*24:02:31
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ABSTRACT:
PROVIDER: PRJEB36269 | ENA |
REPOSITORIES: ENA
Similar Datasets
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Project description:HLA-B*40:02 is one of a few Major Histocompatibility Complex class I (MHC-I) molecules associated with ankylosing spondylitis (AS) independently of HLA-B*27. The endoplasmic reticulum aminopeptidase 2 (ERAP2), an enzyme that process MHC-I ligands and preferentially trims N-terminal basic residues, is also a risk factor for this disease. Like HLA-B*27 and other AS-associated MHC-I molecules, HLA-B*40:02 binds a relatively high percentage of peptides with ERAP2-susceptible residues. In this study the effects of ERAP2 depletion on the HLA-B*40:02 peptidome were analyzed. ERAP2 protein expression was knocked out by CRISPR in the transfectant cell line C1R-B*40:02 and the differences between the peptidomes from the wildtype and ERAP2-KO cells were determined by label-free quantitative comparisons. The qualitative changes dependent on ERAP2 affected about 5% of the peptidome, but quantitative changes in peptide amounts were much more substantial, reflecting a significant influence of this enzyme on the generation/destruction balance of HLA-B*40:02 ligands. As in HLA-B*27, a major effect was on the frequencies of N-terminal residues. In this position basic and small residues were increased in the absence of ERAP2 and aliphatic/aromatic residues were increased in the presence of the enzyme. Since most of the non-B*27 MHC-I molecules associated with AS risk also bind a relatively high percentage of peptides with N-terminal basic residues we hypothesize that the non-epistatic association of ERAP2 with AS might be related to the processing of peptides with these residues bound by AS-associated MHC-I molecules.
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Project description:Analysis of peptide presentation by Human Leukocyte Antigen (HLA) class I of influenza B infected C1R cells expressing HLA-B*07:02, -B*08:01 or -B*35:01.
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Project description:Mass-spectrometry based immunopeptidomics has provided unprecedented insights into antigen presentation, not only charting an enormous ligandome of self-antigens, but also cancer neo-antigens and peptide antigens harbouring post-translational modifications. Here we concentrate on the latter, focusing on the small subset of HLA Class I peptides (less than 1%) that has been observed to be post-translationally modified (PTM) by a O-linked N-acetylglucosamine (GlcNAc). Just like neo-antigens these modified antigens may have specific immunomodulatory functions. Here we compiled from literature, and a new dataset originating from JY B cell lymphoblastoid line cells, a concise albeit comprehensive list of O-GlcNAcylated HLA class I peptides. The cumulative list of O-GlcNAcylated HLA peptides originates from diverse datasets, entailing normal and cancer cell lines as well as tissue samples. Interestingly, the overlap in detected O-GlcNAcylated HLA peptides as well as their source proteins is strikingly high. From the compiled list we extract that O-GlcNAcylated HLA Class I peptides are preferentially presented by the HLA-B07:02 allele. This allele accommodates a Proline anchoring site at position 2, and a binding groove that can accommodate the recently proposed consensus sequence for O-GlcNAcylation, P(V/A/T/S)g(S/T). Most of the O-GlcNAcylated HLA peptides originate from nuclear proteins, notably transcription factors. The conclusions drawn from the compiled list, may assist to predict novel O-GlcNAcylated HLA antigens, which will likely be presented best by patients harbouring HLA-B7:02, or related, alleles that uses Proline as anchoring residue.
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