Removing celiac disease-related gluten proteins from bread wheat while retaining technological roperties: a study with Chinese Spring deletion Lines

H.C. van den Broeck, T.W.J.M. van Herpen, C. Schuit, E.M.J. Salentijn

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Background - 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. 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). Results - The 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 ¿-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 ¿-gliadin, ¿-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. Conclusion - The 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
Original languageEnglish
Article number41
JournalBMC Plant Biology
Publication statusPublished - 2009



  • molecular-weight subunits
  • triticum-aestivum
  • storage proteins
  • alpha-gliadin
  • autoimmune disorders
  • polymeric protein
  • biochemical basis
  • flour properties
  • omega-gliadin
  • gamma-gliadin

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