Abstract

BackgroundGluten proteins can induce celiac disease (CD) in genetically susceptible individuals. In CD patients gluten-derived peptides are presented to the immune system, which leads to a CD4+ T-cell mediated immune response and inflammation of the small intestine. However, not all gluten proteins contain T-cell stimulatory epitopes. Gluten proteins are encoded by multigene loci present on chromosomes 1 and 6 of the three different genomes of hexaploid bread wheat (Triticum aestivum) (AABBDD).ResultsThe effects of deleting individual gluten loci on both the level of T-cell stimulatory epitopes in the gluten proteome and the technological properties of the flour were analyzed using a set of deletion lines of Triticum aestivum cv. Chinese Spring. The reduction of T-cell stimulatory epitopes was analyzed using monoclonal antibodies that recognize T-cell epitopes present in gluten proteins. The deletion lines were technologically tested with respect to dough mixing properties and dough rheology. The results show that removing the α-gliadin locus from the short arm of chromosome 6 of the D-genome (6DS) resulted in a significant decrease in the presence of T-cell stimulatory epitopes but also in a significant loss of technological properties. However, removing the ω-gliadin, γ-gliadin, and LMW-GS loci from the short arm of chromosome 1 of the D-genome (1DS) removed T-cell stimulatory epitopes from the proteome while maintaining technological properties.ConclusionThe consequences of these data are discussed with regard to reducing the load of T-cell stimulatory epitopes in wheat, and to contributing to the design of CD-safe wheat varieties.

Highlights

  • Gluten proteins can induce celiac disease (CD) in genetically susceptible individuals

  • It was observed that the mAb and T-cell minimal sequences were specific for the epitopes in each of the expected protein group, with the exception of the mAb recognizing Glia-α9, whose minimally recognized sequence was present in a number of γ- and ω-gliadin proteins

  • The minimal sequences recognized by mAbs LMW-1 and LMW-2 were more frequently found in the low molecular weight glutenin subunits (LMW-GS) group than the sequence recognized by the corresponding T-cells

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Summary

Introduction

Gluten proteins can induce celiac disease (CD) in genetically susceptible individuals. In CD patients gluten-derived peptides are presented to the immune system, which leads to a CD4+ T-cell mediated immune response and inflammation of the small intestine. Not all gluten proteins contain T-cell stimulatory epitopes. Celiac disease (CD) is a disorder that is characterized by a permanent intolerance to gluten proteins from wheat, rye, and barley. Several native gluten peptides can bind directly to specific human leukocyte antigen (HLA)-DQ2 or DQ8 receptors on antigen presenting cells (APCs). The gluten peptides can be presented by APCs to gluten-sensitive T-cell lymphocytes leading to the release of cytokines, which will cause inflammation reactions and result in damaged intestinal villi [2]

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