ArticleNature structural & molecular biology2014
T-cell receptor recognition of HLA-DQ2-gliadin complexes associated with celiac disease.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
97 citing papers in PubMed, 194 citations in OpenAlex.
- Epitope-specific immunotherapy targeting CD4-positive T cells in coeliac disease: two randomised, double-blind, placebo-controlled phase 1 studies.The lancet. Gastroenterology & hepatology · 2017Trial
- Structural Basis for Clonal Diversity of the Public T Cell Response to a Dominant Human Cytomegalovirus Epitope.The Journal of biological chemistry · 2015Trial
- Gliadin-specific CD4Science advances · 2026Article
- Naïve adaptive immune receptor repertoires in celiac disease assessed by machine learning; impact of the HLA-DQ2.5 allotype on the TCR repertoire.Immunogenetics · 2026Article
- Harnessing gut microbiome enzymes:Microbiology spectrum · 2026Article
- A multi-ethnic reference map of T cell receptor germline diversity reveals evidence of natural selection on alpha chain genes.Nature communications · 2026Article
- Article
- TRBC2-targeting antibody-drug conjugates for the treatment of T cell cancers.Nature cancer · 2025Article
- A dendritic cell population responsible for transglutaminase 2-mediated gluten antigen presentation in celiac disease.JCI insight · 2025Article
- Immune-epithelial-stromal networks define the cellular ecosystem of the small intestine in celiac disease.Nature immunology · 2025Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Nature communications · 2025Article
- Antigen-specific modulation of chronic experimental autoimmune encephalomyelitis in humanized mice by TCR-like antibody targeting autoreactive T-cell epitope.Life science alliance · 2025Article
- The changes induced by hydrodynamic cavitation treatment in wheat gliadin and celiac-toxic peptides.Journal of food science and technology · 2024Article
- A20 haploinsufficiency disturbs immune homeostasis and drives the transformation of lymphocytes with permissive antigen receptors.Science advances · 2024Article
- Posttranslationally modified self-peptides promote hypertension in mouse models.The Journal of clinical investigation · 2024Article
- Article
- The molecular basis underlying T cell specificity towards citrullinated epitopes presented by HLA-DR4.Nature communications · 2024Article
- T-FINDER: A highly sensitive, pan-HLA platform for functional T cell receptor and ligand discovery.Science advances · 2024Article
- 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
37 more citing papers are in PubMed but not listed here.
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Authors and funding
18 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Celiac disease is a T cell-mediated disease induced by dietary gluten, a component of which is gliadin. 95% of individuals with celiac disease carry the HLA (human leukocyte antigen)-DQ2 locus. Here we determined the T-cell receptor (TCR) usage and fine specificity of patient-derived T-cell clones specific for two epitopes from wheat gliadin, DQ2.5-glia-α1a and DQ2.5-glia-α2. We determined the ternary structures of four distinct biased TCRs specific for those epitopes. All three TCRs specific for DQ2.5-glia-α2 docked centrally above HLA-DQ2, which together with mutagenesis and affinity measurements provided a basis for the biased TCR usage. A non-germline encoded arginine residue within the CDR3β loop acted as the lynchpin within this common docking footprint. Although the TCRs specific for DQ2.5-glia-α1a and DQ2.5-glia-α2 docked similarly, their interactions with the respective gliadin determinants differed markedly, thereby providing a basis for epitope specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.