NDLI: HLA-DQ molecules as affinity matrix for identification of gluten T cell epitopes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fallang, Lars-Egil Christophersen, Asbjørn Sollid, Ludvig M. de Souza, Gustavo A. Stamnaes, Jorunn Dørum, Siri Bergseng, Elin Johannesen, Marie K. Qiao, Shuo-Wang Bodd, Michael
Description	Author Affiliation: Dørum S ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Bodd M ( Centre for Immune Regulation, Department of Immunology, Oslo University Hospital-Rikshospitalet, 0424 Oslo, Norway.); Fallang LE ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Bergseng E ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Christophersen A ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Johannesen MK ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Qiao SW ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Stamnaes J ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); de Souza GA ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway); Sollid LM ( Centre for Immune Regulation, Department of Immunology, University of Oslo, 0424 Oslo, Norway)
Abstract	Even though MHC class II is a dominant susceptibility factor for many diseases, culprit T cell epitopes presented by disease-associated MHC molecules remain largely elusive. T cells of celiac disease lesions recognize cereal gluten epitopes presented by the disease-associated HLA molecules DQ2.5, DQ2.2, or DQ8. Employing celiac disease and complex gluten Ag digests as a model, we tested the feasibility of using DQ2.5 and DQ2.2 as an affinity matrix for identification of disease-relevant T cell epitopes. Known gluten T cell epitope peptides were enriched by DQ2.5, whereas a different set of peptides was enriched by DQ2.2. Of 86 DQ2.2-enriched peptides, four core sequences dominated. One of these core sequences is a previously known epitope and two others are novel epitopes. The study provides insight into the selection of gluten epitopes by DQ2.2. Furthermore, the approach presented is relevant for epitope identification in other MHC class II-associated disorders.
ISSN	00221767
e-ISSN	15506606
Journal	The Journal of Immunology
Issue Number	9
Volume Number	193
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2014-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Epitope Mapping Epitopes, T-lymphocyte Immunology Glutens Hla-dq Antigens T-lymphocytes Amino Acid Sequence Celiac Disease Cell Line Chromatography, Gel Gliadin Chemistry Peptides Protein Binding Triticum Research Support, Non-u.s. Gov't Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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