The epitopes in wheat proteins for defining toxic units relevant to human health

Juhász, Angéla; Gell, Gyöngyvér; Békés, F.; Balázs, Ervin

doi:10.1007/s10142-012-0302-3

Cited by 20 publications

(7 citation statements)

References 46 publications

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“…A complex mix of proteins and starch are the two broad components in wheat kernel responsible for dough properties that determine the end-use quality of common wheat. Wheat grain proteins have been classified into three major groups: Glutenin, Gliadins, Albumins/Globulins, with each group comprised of suites of individual polypeptides (Juhász, Gell, Békés, & Balázs, 2012).…”

Section: Introductionmentioning

confidence: 99%

Protein-transitions in and out of the dough matrix in wheat flour mixing

et al. 2017

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Sequential protein behavior in the wheat dough matrix under continuous mixing and heating treatment has been studied using Mixolab-dough samples from two Australian wheat cultivars, Westonia and Wyalkatchem. Size exclusion high performance liquid chromatography (SE-HPLC) and two-dimensional gel electrophoresis (2-DGE) analysis indicated that 32min (80°C) was a critical time point in forming large protein complexes and loosing extractability of several protein groups like y-type high molecular weight glutenin subunits (HMW-GSs), gamma-gliadins, beta-amylases, serpins, and metabolic proteins with higher mass. Up to 32min (80°C) Westonia showed higher protein extractability compared to Wyalkatchem although it was in the opposite direction thereafter. Twenty differentially expressed proteins could be assigned to chromosomes 1D, 3A, 4A, 4B, 4D, 6A, 6B, 7A and 7B. The results expanded the range of proteins associated with changes in the gluten-complex during processing and provided targets for selecting new genetic variants associated with altered quality attributes of the flour.

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Section: Introductionmentioning

confidence: 99%

Protein-transitions in and out of the dough matrix in wheat flour mixing

et al. 2017

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“…Since most CD and WDEIA epitopes contain high proportions of glutamine and proline, it is easy to see that even small differences in the sequences of these proteins among cultivars can affect the number of CD epitopes and impact the immunogenic potential of the flour. The proportions of the different proteins in the flour also must be considered ( Juhász et al, 2012 ). However, quantitative proteomic data for Xioayan 81 was not reported so these comparisons cannot be made.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat

et al. 2018

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Wheat gliadins are a complex group of proteins that contribute to the functional properties of wheat flour doughs and contain epitopes that are relevant for celiac disease (CD) and wheat-dependent exercise-induced anaphylaxis (WDEIA). In this study, we extracted ethanol-soluble gliadin fractions from flour of the Korean bread wheat cultivar Keumkang. Proteins were separated by 2-dimensional gel electrophoresis (2-DE) using a pI range of 6–11 in the first dimension and subjected to tandem mass spectrometry. α-, γ-, and ω-gliadins were identified as the predominant proteins in 31, 28, and one 2-DE spot, respectively. An additional six ω-gliadins were identified in a separate experiment in which a pI range of 3–11 was used for protein separation. We analyzed the composition of CD- and WDEIA-relevant epitopes in the gliadin sequences from Keumkang flour, demonstrating the immunogenic potential of this cultivar. Detailed knowledge about the complement of gliadins accumulated in Keumkang flour provides the background necessary to devise either breeding or biotechnology strategies to improve the functional properties and reduce the adverse health effects of the flour.

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“…Based on our previous studies a high number cereal grain proteins may contain peptides rich in proline and glutamine making them a target for celiac disease-related antigen presenting cells and immunoglobulins101524. In wheat, the majority of these proteins belong to the prolamin superfamily and are a natural compound of the wheat gluten.…”

Section: Discussionmentioning

confidence: 99%

Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease

Gell

Kovács

Veres

et al. 2017

Sci Rep

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Brachypodium distachyon, a small annual grass with seed storage globulins as primary protein reserves was used in our study to analyse the toxic nature of non-prolamin seed storage proteins related to celiac disease. The main storage proteins of B. distachyon are the 7S globulin type proteins and the 11S, 12S seed storage globulins similar to oat and rice. Immunoblot analyses using serum samples from celiac disease patients were carried out followed by the identification of immune-responsive proteins using mass spectrometry. Serum samples from celiac patients on a gluten-free diet, from patients with Crohn’s disease and healthy subjects, were used as controls. The identified proteins with intense serum-IgA reactivity belong to the 7S and 11–12S seed globulin family. Structure prediction and epitope predictions analyses confirmed the presence of celiac disease-related linear B cell epitope homologs and the presence of peptide regions with strong HLA-DQ8 and DQ2 binding capabilities. These results highlight that both MHC-II presentation and B cell response may be developed not only to prolamins but also to seed storage globulins. This is the first study of the non-prolamin type seed storage proteins of Brachypodium from the aspect of the celiac disease.

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The epitopes in wheat proteins for defining toxic units relevant to human health

Cited by 20 publications

References 46 publications

Protein-transitions in and out of the dough matrix in wheat flour mixing

Protein-transitions in and out of the dough matrix in wheat flour mixing

Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat

Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease

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