ArticleThe Journal of biological chemistry2015
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Separate Gut Plasma Cell Populations Produce Auto-Antibodies against Transglutaminase 2 and Transglutaminase 3 in Dermatitis Herpetiformis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Single-cell approaches to dissect adaptive immune responses involved in autoimmunity: the case of celiac disease.Mucosal immunology · 2022Review
- Society for the Study of Celiac Disease position statement on gaps and opportunities in coeliac disease.Nature reviews. Gastroenterology & hepatology · 2021Article
- Structural basis of a shared antibody response to SARS-CoV-2.Science (New York, N.Y.) · 2020Article
- Transglutaminase 2-Mediated p53 Depletion Promotes Angiogenesis by Increasing HIF-1α-p300 Binding in Renal Cell Carcinoma.International journal of molecular sciences · 2020Article
- Structures of Human Transglutaminase 2: Finding Clues for Interference in Cross-linking Mediated Activity.International journal of molecular sciences · 2020Review
- B cell tolerance and antibody production to the celiac disease autoantigen transglutaminase 2.The Journal of experimental medicine · 2020Article
- Anti-type 2 transglutaminase antibodies as modulators of type 2 transglutaminase functions: a possible pathological role in celiac disease.Cellular and molecular life sciences : CMLS · 2018Review
- Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity.PloS one · 2018Article
- Transglutaminase-2 promotes metastatic and stem-like phenotypes in osteosarcoma.American journal of cancer research · 2018Article
- Strong Clonal Relatedness between Serum and Gut IgA despite Different Plasma Cell Origins.Cell reports · 2017Article
- Progress in small-angle scattering from biological solutions at high-brilliance synchrotrons.IUCrJ · 2017Review
- New Insights into the Pathogenesis of Celiac Disease.Frontiers in medicine · 2017Review
- Multivalent pIX phage display selects for distinct and improved antibody properties.Scientific reports · 2016Article
- Epitope-dependent Functional Effects of Celiac Disease Autoantibodies on Transglutaminase 2.The Journal of biological chemistry · 2016Article
- Lack of evidence of rotavirus-dependent molecular mimicry as a trigger of coeliac disease.Clinical and experimental immunology · 2016Article
- Recent Advances in Celiac Disease from TTG to Gluten in Pee.Clinical and translational gastroenterology · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Antibodies to the autoantigen transglutaminase 2 (TG2) are a hallmark of celiac disease. We have studied the interaction between TG2 and an anti-TG2 antibody (679-14-E06) derived from a single gut IgA plasma cell of a celiac disease patient. The antibody recognizes one of four identified epitopes targeted by antibodies of plasma cells of the disease lesion. The binding interface was identified by small angle x-ray scattering, ab initio and rigid body modeling using the known crystal structure of TG2 and the crystal structure of the antibody Fab fragment, which was solved at 2.4 Å resolution. The result was confirmed by testing binding of the antibody to TG2 mutants by ELISA and surface plasmon resonance. TG2 residues Arg-116 and His-134 were identified to be critical for binding of 679-14-E06 as well as other epitope 1 antibodies. In contrast, antibodies directed toward the two other main epitopes (epitopes 2 and 3) were not affected by these mutations. Molecular dynamics simulations suggest interactions of 679-14-E06 with the N-terminal domain of TG2 via the CDR2 and CDR3 loops of the heavy chain and the CDR2 loop of the light chain. In addition there were contacts of the framework 3 region of the heavy chain with the catalytic domain of TG2. The results provide an explanation for the biased usage of certain heavy and light chain gene segments by epitope 1-specific antibodies in celiac disease.
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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.