Transcriptomic analysis of intestine following administration of a transglutaminase 2 inhibitor to prevent gluten-induced intestinal damage in celiac disease.


Journal

Nature immunology
ISSN: 1529-2916
Titre abrégé: Nat Immunol
Pays: United States
ID NLM: 100941354

Informations de publication

Date de publication:
24 Jun 2024
Historique:
received: 22 06 2023
accepted: 13 05 2024
medline: 25 6 2024
pubmed: 25 6 2024
entrez: 24 6 2024
Statut: aheadofprint

Résumé

Transglutaminase 2 (TG2) plays a pivotal role in the pathogenesis of celiac disease (CeD) by deamidating dietary gluten peptides, which facilitates antigenic presentation and a strong anti-gluten T cell response. Here, we elucidate the molecular mechanisms underlying the efficacy of the TG2 inhibitor ZED1227 by performing transcriptional analysis of duodenal biopsies from individuals with CeD on a long-term gluten-free diet before and after a 6-week gluten challenge combined with 100 mg per day ZED1227 or placebo. At the transcriptome level, orally administered ZED1227 effectively prevented gluten-induced intestinal damage and inflammation, providing molecular-level evidence that TG2 inhibition is an effective strategy for treating CeD. ZED1227 treatment preserved transcriptome signatures associated with mucosal morphology, inflammation, cell differentiation and nutrient absorption to the level of the gluten-free diet group. Nearly half of the gluten-induced gene expression changes in CeD were associated with the epithelial interferon-γ response. Moreover, data suggest that deamidated gluten-induced adaptive immunity is a sufficient step to set the stage for CeD pathogenesis. Our results, with the limited sample size, also suggest that individuals with CeD might benefit from an HLA-DQ2/HLA-DQ8 stratification based on gene doses to maximally eliminate the interferon-γ-induced mucosal damage triggered by gluten.

Identifiants

pubmed: 38914866
doi: 10.1038/s41590-024-01867-0
pii: 10.1038/s41590-024-01867-0
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Academy of Finland (Suomen Akatemia)
ID : 310011

Investigateurs

Karin Kull (K)
Jari Koskenpato (J)
Mika Scheinin (M)
Marja-Leena Lähdeaho (ML)
Michael Schumann (M)
Yurdagül Zopf (Y)
Andreas Stallmach (A)
Ansgar W Lohse (AW)
Stefano Fusco (S)
Jost Langhorst (J)
Helga Paula Török (HP)
Valerie Byrnes (V)
Juozas Kupcinskas (J)
Øistein Hovde (Ø)
Jørgen Jahnsen (J)
Luc Biedermann (L)
Jonas Zeitz (J)

Informations de copyright

© 2024. The Author(s).

Références

King, J. A. et al. Incidence of celiac disease is increasing over time: a systematic review and meta-analysis. Am. J. Gastroenterol. 115, 507–525 (2020).
pubmed: 32022718
Lebwohl, B., Sanders, D. S. & Green, P. H. R. Coeliac disease. Lancet 391, 70–81 (2018).
pubmed: 28760445
Leffler, D. A., Green, P. H. R. & Fasano, A. Extraintestinal manifestations of coeliac disease. Nat. Rev. Gastroenterol. Hepatol. 12, 561–571 (2015).
pubmed: 26260366
Kahaly, G. J., Frommer, L. & Schuppan, D. Celiac disease and endocrine autoimmunity—the genetic link. Autoimmun. Rev. 17, 1169–1175 (2018).
pubmed: 30316996
Syage, J. A. et al. Determination of gluten consumption in celiac disease patients on a gluten-free diet. Am. J. Clin. Nutr. 107, 201–207 (2018).
pubmed: 29529159
Silvester, J. A. et al. Most patients with celiac disease on gluten-free diets consume measurable amounts of gluten. Gastroenterology 158, 1497–1499 (2020).
pubmed: 31866245
Roos, S., Liedberg, G. M., Hellström, I. & Wilhelmsson, S. Persistent symptoms in people with celiac disease despite gluten-free diet: a concern? Gastroenterol. Nurs. 42, 496–503 (2019).
pubmed: 31770352
van Megen, F. et al. High disease burden in treated celiac patients—a web-based survey. Scand. J. Gastroenterol. 56, 882–888 (2021).
pubmed: 34057009
Itzlinger, A., Branchi, F., Elli, L. & Schumann, M. Gluten-free diet in celiac disease—forever and for all? Nutrients 10, 1796 (2018).
pubmed: 30453686 pmcid: 6267495
Daveson, A. J. M. et al. Baseline quantitative histology in therapeutics trials reveals villus atrophy in most patients with coeliac disease who appear well controlled on gluten‐free diet. GastroHep 2, 22–30 (2020).
Kreutz, J. M., Adriaanse, M. P. M., van der Ploeg, E. M. C. & Vreugdenhil, A. C. E. Nutrient deficiencies in adults and children with treated and untreated celiac disease. Nutrients 12, 500 (2020).
pubmed: 32075276 pmcid: 7071237
Vici, G., Belli, L., Biondi, M. & Polzonetti, V. Gluten free diet and nutrient deficiencies: a review. Clin. Nutr. 35, 1236–1241 (2016).
pubmed: 27211234
Dotsenko, V. et al. Genome-wide transcriptomic analysis of intestinal mucosa in celiac disease patients on a gluten-free diet and postgluten challenge. Cell. Mol. Gastroenterol. Hepatol. 11, 13–32 (2021).
pubmed: 32745639
Dieterich, W. et al. Identification of tissue transglutaminase as the autoantigen of celiac disease. Nat. Med. 3, 797–801 (1997).
pubmed: 9212111
Molberg, Ø. et al. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat. Med. 4, 713–717 (1998).
pubmed: 9623982
van de Wal, Y. et al. Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity. J. Immunol. 161, 1585–1588 (1998).
pubmed: 9712018
Lundin, K. E. A. & Sollid, L. M. Advances in coeliac disease. Curr. Opin. Gastroenterol. 30, 154–162 (2014).
pubmed: 24457347
Schuppan, D., Junker, Y. & Barisani, D. Celiac disease: from pathogenesis to novel therapies. Gastroenterology 137, 1912–1933 (2009).
pubmed: 19766641
Schuppan, D. et al. A randomized trial of a transglutaminase 2 inhibitor for celiac disease. N. Engl. J. Med. 385, 35–45 (2021).
pubmed: 34192430
Vader, W. et al. The HLA-DQ2 gene dose effect in celiac disease is directly related to the magnitude and breadth of gluten-specific T cell responses. Proc. Natl Acad. Sci. USA 100, 12390–12395 (2003).
pubmed: 14530392 pmcid: 218768
Koning, F. Celiac disease: quantity matters. Semin. Immunopathol. 34, 541–549 (2012).
pubmed: 22732901 pmcid: 3410019
Busslinger, G. A. et al. Human gastrointestinal epithelia of the esophagus, stomach, and duodenum resolved at single-cell resolution. Cell Rep. 34, 108819 (2021).
pubmed: 33691112
Törönen, P., Ojala, P. J., Marttinen, P. & Holm, L. Robust extraction of functional signals from gene set analysis using a generalized threshold free scoring function. BMC Bioinformatics 10, 307 (2009).
pubmed: 19775443 pmcid: 2761411
DiRaimondo, T. R., Klöck, C. & Khosla, C. Interferon-γ activates transglutaminase 2 via a phosphatidylinositol-3-kinase-dependent pathway: implications for celiac sprue therapy. J. Pharmacol. Exp. Ther. 341, 104–114 (2012).
pubmed: 22228808 pmcid: 3310700
Fina, D. et al. Interleukin 21 contributes to the mucosal T helper cell type 1 response in coeliac disease. Gut 57, 887–892 (2008).
pubmed: 17965065
Büchold, C. et al. Features of ZED1227: the first-in-class tissue transglutaminase inhibitor undergoing clinical evaluation for the treatment of celiac disease. Cells 11, 1667 (2022).
pubmed: 35626704 pmcid: 9139979
Isola, J. et al. The oral transglutaminase 2 inhibitor ZED1227 accumulates in the villous enterocytes in celiac disease patients during gluten challenge and drug treatment. Int. J. Mol. Sci. 24, 10815 (2023).
pubmed: 37445994 pmcid: 10341493
Pascual, G. et al. A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-γ. Nature 437, 759–763 (2005).
pubmed: 16127449 pmcid: 1464798
Bailey, S. T. & Ghosh, S. ‘PPAR’ting ways with inflammation. Nat. Immunol. 6, 966–967 (2005).
pubmed: 16177802
Simula, M. P. et al. PPAR signaling pathway and cancer-related proteins are involved in celiac disease-associated tissue damage. Mol. Med. 16, 199–209 (2010).
pubmed: 20454521 pmcid: 2864807
Luciani, A. et al. Lysosomal accumulation of gliadin p31-43 peptide induces oxidative stress and tissue transglutaminase-mediated PPARgamma downregulation in intestinal epithelial cells and coeliac mucosa. Gut 59, 311–319 (2010).
pubmed: 19951908
Daynes, R. A. & Jones, D. C. Emerging roles of PPARS in inflammation and immunity. Nat. Rev. Immunol. 2, 748–759 (2002).
pubmed: 12360213
ter Steege, J., Buurman, W., Arends, J. W. & Forget, P. Presence of inducible nitric oxide synthase, nitrotyrosine, CD68, and CD14 in the small intestine in celiac disease. Lab. Investig. J. Tech. Methods Pathol. 77, 29–36 (1997).
Maiuri, M. C. et al. Gliadin increases iNOS gene expression in interferon-γ-stimulated RAW 264.7 cells through a mechanism involving NF-κB. Naunyn. Schmiedebergs Arch. Pharmacol. 368, 63–71 (2003).
pubmed: 12845421
Daniels, I., Cavill, D., Murray, I. A. & Long, R. G. Elevated expression of iNOS mRNA and protein in coeliac disease. Clin. Chim. Acta 356, 134–142 (2005).
pubmed: 15936309
Murray, I. A., Bullimore, D. W. & Long, R. G. Fasting plasma nitric oxide products in coeliac disease. Eur. J. Gastroenterol. Hepatol. 15, 1091–1095 (2003).
pubmed: 14501617
Diefenbach, A., Schindler, H., Röllinghoff, M., Yokoyama, W. M. & Bogdan, C. Requirement for type 2 NO synthase for IL-12 signaling in innate immunity. Science 284, 951–955 (1999).
pubmed: 10320373
Orenbuch, R. et al. arcasHLA: high-resolution HLA typing from RNAseq. Bioinformatics 36, 33–40 (2020).
pubmed: 31173059
Tollefsen, S. et al. HLA-DQ2 and -DQ8 signatures of gluten T cell epitopes in celiac disease. J. Clin. Invest. 116, 2226–2236 (2006).
pubmed: 16878175 pmcid: 1518792
Tollefsen, S. et al. Structural and functional studies of trans-encoded HLA-DQ2.3 (DQA1*03:01/DQB1*02:01) protein molecule. J. Biol. Chem. 287, 13611–13619 (2012).
pubmed: 22362761 pmcid: 3340161
Senger, S. et al. Celiac disease histopathology recapitulates Hedgehog downregulation, consistent with wound healing processes activation. PLoS ONE 10, e0144634 (2015).
pubmed: 26649570 pmcid: 4674131
Juuti-Uusitalo, K., Mäki, M., Kainulainen, H., Isola, J. & Kaukinen, K. Gluten affects epithelial differentiation-associated genes in small intestinal mucosa of coeliac patients. Clin. Exp. Immunol. 150, 294–305 (2007).
pubmed: 17888028 pmcid: 2219351
Nanayakkara, M., Lania, G., Maglio, M., Kosova, R. & Sarno, M. Enterocyte proliferation and signaling are constitutively altered in celiac disease. PLoS ONE 8, 76006 (2013).
Halstensen, T. S. & Brandtzaeg, P. Activated T lymphocytes in the celiac lesion: non-proliferative activation (CD25) of CD4
pubmed: 8094672
Kutlu, T. et al. Numbers of T cell receptor (TCR) αβ
pubmed: 8432475 pmcid: 1373972
Laforenza, U. et al. Solute transporters and aquaporins are impaired in celiac disease. Biol. Cell 102, 457–467 (2010).
pubmed: 20415666
Banaganapalli, B. et al. Exploring celiac disease candidate pathways by global gene expression profiling and gene network cluster analysis. Sci. Rep. 10, 16290 (2020).
pubmed: 33004927 pmcid: 7529771
Barone, M. V. et al. Growth factor-like activity of gliadin, an alimentary protein: implications for coeliac disease. Gut 56, 480–488 (2007).
pubmed: 16891357 pmcid: 1856836
Maiuri, L. et al. Association between innate response to gliadin and activation of pathogenic T cells in coeliac disease. Lancet 362, 30–37 (2003).
pubmed: 12853196
Bragde, H., Jansson, U., Fredrikson, M., Grodzinsky, E. & Söderman, J. Celiac disease biomarkers identified by transcriptome analysis of small intestinal biopsies. Cell. Mol. Life Sci. 75, 4385–4401 (2018).
pubmed: 30097691 pmcid: 6208765
van der Graaf, A. et al. Systematic prioritization of candidate genes in disease loci identifies TRAFD1 as a master regulator of IFNγ signaling in celiac disease. Front. Genet. 11, 562434 (2020).
pubmed: 33569077
Bajor, J. et al. Classical celiac disease is more frequent with a double dose of HLA-DQB1*02: a systematic review with meta-analysis. PLoS ONE 14, e0212329 (2019).
pubmed: 30763397 pmcid: 6375622
Al-Toma, A. et al. Human leukocyte antigen-DQ2 homozygosity and the development of refractory celiac disease and enteropathy-associated T-cell lymphoma. Clin. Gastroenterol. Hepatol. Off. Clin. Pract. J. Am. Gastroenterol. Assoc. 4, 315–319 (2006).
Nijeboer, P., van Wanrooij, R. L. J., Tack, G. J., Mulder, C. J. J. & Bouma, G. Update on the diagnosis and management of refractory coeliac disease. Gastroenterol. Res. Pract. 2013, 518483 (2013).
pubmed: 23762036 pmcid: 3665175
Waite, K. J., Floyd, Z. E., Arbour-Reily, P. & Stephens, J. M. Interferon-gamma-induced regulation of peroxisome proliferator-activated receptor gamma and STATs in adipocytes. J. Biol. Chem. 276, 7062–7068 (2001).
pubmed: 11106650
Wapenaar, M. C. et al. The interferon gamma gene in celiac disease: augmented expression correlates with tissue damage but no evidence for genetic susceptibility. J. Autoimmun. 23, 183–190 (2004).
pubmed: 15324937
Guennouni, M. et al. Gluten contamination in labelled gluten-free, naturally gluten-free and meals in food services in low-, middle- and high-income countries: a systematic review and meta-analysis. Br. J. Nutr. 127, 1528–1542 (2022).
pubmed: 34753529
Atlasy, N. et al. Single cell transcriptomic analysis of the immune cell compartment in the human small intestine and in celiac disease. Nat. Commun. 13, 4920 (2022).
pubmed: 35995787 pmcid: 9395525
Clinical Trials Register. https://www.clinicaltrialsregister.eu/ctr-search/trial/2017-002241-30/LT
Taavela, J. et al. Validation of morphometric analyses of small-intestinal biopsy readouts in celiac disease. PLoS ONE 8, e76163 (2013).
pubmed: 24146832 pmcid: 3795762
Sato, T. et al. Long-term expansion of epithelial organoids from human colon, adenoma, adenocarcinoma, and Barrett’s epithelium. Gastroenterology 141, 1762–1772 (2011).
pubmed: 21889923
Dotsenko, V., Sioofy-Khojine, A.-B., Hyöty, H. & Viiri, K. Human intestinal organoid models for celiac disease research. in Methods in Cell Biology (Academic Press, 2023). https://doi.org/10.1016/bs.mcb.2023.01.008
Taavela, J. et al. Histological, immunohistochemical and mRNA gene expression responses in coeliac disease patients challenged with gluten using PAXgene fixed paraffin-embedded duodenal biopsies. BMC Gastroenterol. 19, 189 (2019).
pubmed: 31730447 pmcid: 6858741
Love, M. I., Huber, W. & Anders, S. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol. 15, 550 (2014).
pubmed: 25516281 pmcid: 4302049
Benjamini, Y. & Hochberg, Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. Ser. B Methodol. 57, 289–300 (1995).
Alexa, A. & Rahnenfuhrer, J. topGO: enrichment analysis for Gene Ontology. (2022).
Yu, G. & He, Q.-Y. ReactomePA: an R/Bioconductor package for Reactome pathway analysis and visualization. Mol. Biosyst. 12, 477–479 (2016).
pubmed: 26661513
Törönen, P., Ojala, P. J., Marttinen, P. & Holm, L. BMC Bioinformatics Robust extraction of functional signals from gene set analysis using a generalized threshold free scoring function. (2009) https://doi.org/10.1186/1471-2105-10-307
Mishra, P. & Holm, L. Gene expression Gene set analysis: limitations in popular existing methods and proposed improvements. 30, 2747–2756 (2014).
Wang, X., Park, J., Susztak, K., Zhang, N. R. & Li, M. Bulk tissue cell type deconvolution with multi-subject single-cell expression reference. Nat. Commun. 10, 1–9 (2019).
Elmentaite, R. et al. Cells of the human intestinal tract mapped across space and time. Nat. 2021 5977875 597, 250–255 (2021).
Naito, T. & Okada, Y. HLA imputation and its application to genetic and molecular fine-mapping of the MHC region in autoimmune diseases. Semin. Immunopathol. 44, 15–28 (2022).
pubmed: 34786601
Schmittgen, T. D. & Livak, K. J. Analyzing real-time PCR data by the comparative C
pubmed: 18546601
Folk, J. E. & Cole, P. W. Mechanism of action of guinea pig liver transglutaminase I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. J. Biol. Chem. 241, 5518–5525 (1966).
pubmed: 5928192
Kiviniemi, M. et al. A High-Throughput Population Screening System for the Estimation of Genetic Risk for Type 1 Diabetes: An Application for the TEDDY (The Environmental Determinants of Diabetes in the Young) Study. Diabetes Technol. Ther. 9, 460–472 (2007).
pubmed: 17931054
Lehmusvuori, A., Kiviniemi, M., Ilonen, J. & Soukka, T. Closed-tube human leukocyte antigen DQA1
pubmed: 25120130

Auteurs

Valeriia Dotsenko (V)

Celiac Disease Research Center, Faculty of Medicine and Health Technology, Tampere University and Tampere University Hospital, Tampere, Finland.

Bernhard Tewes (B)

Dr. Falk Pharma GmbH, Freiburg, Germany.

Martin Hils (M)

Zedira GmbH, Darmstadt, Germany.

Ralf Pasternack (R)

Zedira GmbH, Darmstadt, Germany.

Jorma Isola (J)

Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Jilab Inc, Tampere, Finland.

Juha Taavela (J)

Celiac Disease Research Center, Faculty of Medicine and Health Technology, Tampere University and Tampere University Hospital, Tampere, Finland.
Department of Gastroenterology and Alimentary Tract Surgery, Tampere University Hospital, Tampere, Finland.

Alina Popp (A)

Celiac Disease Research Center, Faculty of Medicine and Health Technology, Tampere University and Tampere University Hospital, Tampere, Finland.
University of Medicine and Pharmacy 'Carol Davila' and National Institute for Mother and Child Health, Bucharest, Romania.

Jani Sarin (J)

Jilab Inc, Tampere, Finland.

Heini Huhtala (H)

Unit of Health Sciences, Faculty of Social Sciences, Tampere University, Tampere, Finland.

Pauliina Hiltunen (P)

Department of Pediatrics, Tampere University Hospital, Tampere, Finland.

Timo Zimmermann (T)

Dr. Falk Pharma GmbH, Freiburg, Germany.

Ralf Mohrbacher (R)

Dr. Falk Pharma GmbH, Freiburg, Germany.

Roland Greinwald (R)

Dr. Falk Pharma GmbH, Freiburg, Germany.

Knut E A Lundin (KEA)

Norwegian Coeliac Disease Research Centre, Institute of Clinical Medicine, Faculty of Medicine, University of Oslo, Oslo, Norway.
Department of Gastroenterology, Oslo University Hospital Rikshospitalet, Oslo, Norway.

Detlef Schuppan (D)

Institute of Translational Immunology and Celiac Center, Medical Center, Johannes-Gutenberg University, Mainz, Germany.
Division of Gastroenterology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.

Markku Mäki (M)

Celiac Disease Research Center, Faculty of Medicine and Health Technology, Tampere University and Tampere University Hospital, Tampere, Finland.

Keijo Viiri (K)

Celiac Disease Research Center, Faculty of Medicine and Health Technology, Tampere University and Tampere University Hospital, Tampere, Finland. keijo.viiri@tuni.fi.

Classifications MeSH