ArticleImmunogenetics2015
Different binding motifs of the celiac disease-associated HLA molecules DQ2.5, DQ2.2, and DQ7.5 revealed by relative quantitative proteomics of endogenous peptide repertoires.
Article in Immunogenetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 99 citations in OpenAlex.
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- Peptides Derived from α-Tubulin Induce Functional T Regulatory Cells.International journal of molecular sciences · 2025Article
- Review Article: Novel Enzyme Therapy Design for Gluten Peptide Digestion Through Exopeptidase Supplementation.Alimentary pharmacology & therapeutics · 2025Review
- Immunopeptidomics for autoimmunity: unlocking the chamber of immune secrets.NPJ systems biology and applications · 2025Review
- Evaluation of the Frequency of HLA-DQ2/DQ8 Genes Among Patients with Celiac Disease and Those on a Gluten-Free Diet.Foods (Basel, Switzerland) · 2025Article
- Modeling Peptide-Protein Interactions by a Logo-Based Method: Application in Peptide-HLA Binding Predictions.Molecules (Basel, Switzerland) · 2024Article
- Assessment of Novel Proteins Triggering Celiac Disease via Docking-Based Approach.Molecules (Basel, Switzerland) · 2023Article
- Characterizations of a neutralizing antibody broadly reactive to multiple gluten peptide:HLA-DQ2.5 complexes in the context of celiac disease.Nature communications · 2023Article
- Specific Genetic Polymorphisms Contributing in Differential Binding of Gliadin Peptides to HLA-DQ and TCR to Elicit Immunogenicity in Celiac Disease.Biochemical genetics · 2023Article
- Machine learning reveals limited contribution of trans-only encoded variants to the HLA-DQ immunopeptidome.Communications biology · 2023Article
- What does not look like celiac disease and instead it is.Gastroenterology and hepatology from bed to bench · 2023Article
- Intravenous immunoglobulin induces IgG internalization by tolerogenic myeloid dendritic cells that secrete IL-10 and expand Fc-specific regulatory T cells.Clinical and experimental immunology · 2022Article
- Marking the 50th anniversary of a seminal paper in rheumatology: did Baruj Benacerraf and Hugh McDevitt get it right?Annals of the rheumatic diseases · 2022Article
- Structural aspects of chemical modifications in the MHC-restricted immunopeptidome; Implications for immune recognition.Frontiers in chemistry · 2022Review
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- CSPG4 Is a Potential Therapeutic Target in Anaplastic Thyroid Cancer.Thyroid : official journal of the American Thyroid Association · 2021Article
- Probiotics Supplements Reduce ER Stress and Gut Inflammation Associated with Gliadin Intake in a Mouse Model of Gluten Sensitivity.Nutrients · 2021Article
- IgG Epitopes Processed and Presented by IgGJournal of immunology (Baltimore, Md. : 1950) · 2021Observational
- Gut-Ex-Vivo system as a model to study gluten response in celiac disease.Cell death discovery · 2021Article
- Transmembrane Helices Are an Over-Presented and Evolutionarily Conserved Source of Major Histocompatibility Complex Class I and II Epitopes.Frontiers in immunology · 2021Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Celiac disease is caused by intolerance to cereal gluten proteins, and HLA-DQ molecules are involved in the disease pathogenesis by presentation of gluten peptides to CD4(+) T cells. The α- or β-chain sharing HLA molecules DQ2.5, DQ2.2, and DQ7.5 display different risks for the disease. It was recently demonstrated that T cells of DQ2.5 and DQ2.2 patients recognize distinct sets of gluten epitopes, suggesting that these two DQ2 variants select different peptides for display. To explore whether this is the case, we performed a comprehensive comparison of the endogenous self-peptides bound to HLA-DQ molecules of B-lymphoblastoid cell lines. Peptides were eluted from affinity-purified HLA molecules of nine cell lines and subjected to quadrupole orbitrap mass spectrometry and MaxQuant software analysis. Altogether, 12,712 endogenous peptides were identified at very different relative abundances. Hierarchical clustering of normalized quantitative data demonstrated significant differences in repertoires of peptides between the three DQ variant molecules. The neural network-based method, NNAlign, was used to identify peptide-binding motifs. The binding motifs of DQ2.5 and DQ7.5 concurred with previously established binding motifs. The binding motif of DQ2.2 was strikingly different from that of DQ2.5 with position P3 being a major anchor having a preference for threonine and serine. This is notable as three recently identified epitopes of gluten recognized by T cells of DQ2.2 celiac patients harbor serine at position P3. This study demonstrates that relative quantitative comparison of endogenous peptides sampled from our protein metabolism by HLA molecules provides clues to understand HLA association with disease.
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