دورية أكاديمية
أعرض في EDS

A high-affinity human TCR-like antibody detects celiac disease gluten peptide-MHC complexes and inhibits T cell activation.

التفاصيل البيبلوغرافية
العنوان: A high-affinity human TCR-like antibody detects celiac disease gluten peptide-MHC complexes and inhibits T cell activation.
المؤلفون: Frick R; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; Centre for Immune Regulation and Department of Biosciences, University of Oslo, Oslo, Norway., Høydahl LS; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; Centre for Immune Regulation and Department of Biosciences, University of Oslo, Oslo, Norway.; KG Jebsen Coeliac Disease Research Centre, University of Oslo, Oslo, Norway., Petersen J; Infection and Immunity Program, Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria, Australia.; Australian Research Council Centre of Excellence for Advanced Molecular Imaging, Monash University, Clayton, Victoria, Australia., du Pré MF; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; KG Jebsen Coeliac Disease Research Centre, University of Oslo, Oslo, Norway., Kumari S; Nextera AS, Oslo, Norway., Berntsen G; Nextera AS, Oslo, Norway., Dewan AE; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; KG Jebsen Coeliac Disease Research Centre, University of Oslo, Oslo, Norway., Jeliazkov JR; Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD, USA., Gunnarsen KS; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; Centre for Immune Regulation and Department of Biosciences, University of Oslo, Oslo, Norway., Frigstad T; Nextera AS, Oslo, Norway., Vik ES; Nextera AS, Oslo, Norway., Llerena C; Infection and Immunity Program, Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria, Australia., Lundin KEA; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; KG Jebsen Coeliac Disease Research Centre, University of Oslo, Oslo, Norway.; Department of Gastroenterology, Oslo University Hospital-Rikshospitalet, Oslo, Norway., Yaqub S; Department of Gastrointestinal Surgery, Oslo University Hospital-Rikshospitalet, Oslo, Norway.; Institute of Clinical Medicine, University of Oslo, Oslo, Norway., Jahnsen J; Institute of Clinical Medicine, University of Oslo, Oslo, Norway.; Department of Gastroenterology, Akershus University Hospital, Lørenskog, Norway., Gray JJ; Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD, USA.; Department of Chemical and Biomolecular Engineering and Institute of NanoBioTechnology, Johns Hopkins University, Baltimore, MD, USA.; Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins School of Medicine, Baltimore, MD, USA., Rossjohn J; Infection and Immunity Program, Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria, Australia.; Australian Research Council Centre of Excellence for Advanced Molecular Imaging, Monash University, Clayton, Victoria, Australia.; Institute of Infection and Immunity, Cardiff University School of Medicine, Heath Park, Cardiff, UK., Sollid LM; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; KG Jebsen Coeliac Disease Research Centre, University of Oslo, Oslo, Norway., Sandlie I; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway.; Centre for Immune Regulation and Department of Biosciences, University of Oslo, Oslo, Norway., Løset GÅ; Centre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital-Rikshospitalet, Oslo, Norway. galoset@nextera.no.; Centre for Immune Regulation and Department of Biosciences, University of Oslo, Oslo, Norway.; Nextera AS, Oslo, Norway.
المصدر: Science immunology [Sci Immunol] 2021 Aug 20; Vol. 6 (62).
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101688624 Publication Model: Print Cited Medium: Internet ISSN: 2470-9468 (Electronic) Linking ISSN: 24709468 NLM ISO Abbreviation: Sci Immunol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Association for the Advancement of Science, [2016]-
مواضيع طبية MeSH: CD4-Positive T-Lymphocytes/*immunology , Celiac Disease/*immunology , Glutens/*immunology , HLA-DQ Antigens/*immunology , Peptides/*immunology , Receptors, Antigen, T-Cell/*immunology, Animals ; Cell Line, Tumor ; Epitopes, T-Lymphocyte/immunology ; Glutens/chemistry ; HLA-DQ Antigens/chemistry ; Humans ; Lymphocyte Activation/immunology ; Mice ; Models, Molecular ; Peptides/chemistry ; Receptors, Antigen, T-Cell/chemistry
مستخلص: Antibodies specific for peptides bound to human leukocyte antigen (HLA) molecules are valuable tools for studies of antigen presentation and may have therapeutic potential. Here, we generated human T cell receptor (TCR)-like antibodies toward the immunodominant signature gluten epitope DQ2.5-glia-α2 in celiac disease (CeD). Phage display selection combined with secondary targeted engineering was used to obtain highly specific antibodies with picomolar affinity. The crystal structure of a Fab fragment of the lead antibody 3.C11 in complex with HLA-DQ2.5:DQ2.5-glia-α2 revealed a binding geometry and interaction mode highly similar to prototypic TCRs specific for the same complex. Assessment of CeD biopsy material confirmed disease specificity and reinforced the notion that abundant plasma cells present antigen in the inflamed CeD gut. Furthermore, 3.C11 specifically inhibited activation and proliferation of gluten-specific CD4 + T cells in vitro and in HLA-DQ2.5 humanized mice, suggesting a potential for targeted intervention without compromising systemic immunity.
(Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)
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معلومات مُعتمدة: R01 GM078221 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Epitopes, T-Lymphocyte)
0 (HLA-DQ Antigens)
0 (HLA-DQ2 antigen)
0 (Peptides)
0 (Receptors, Antigen, T-Cell)
8002-80-0 (Glutens)
تواريخ الأحداث: Date Created: 20210821 Date Completed: 20220228 Latest Revision: 20220228
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8670751
DOI: 10.1126/sciimmunol.abg4925
PMID: 34417258
قاعدة البيانات: MEDLINE
الوصف
تدمد:2470-9468
DOI:10.1126/sciimmunol.abg4925