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Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species

1
Departamento de Microbiología y Parasitología, Facultad de Farmacia, Universidad de Sevilla, 41012 Sevilla, Spain
2
Departamento de Mejora Genética Vegetal, Instituto de Agricultura Sostenible (IAS-CSIC), 14004 Córdoba, Spain
3
Departamento de Gastronterología pediátrica, Hospital Virgen de las Nieves, 18014 Granada, Spain
4
Departamento de Biología Experimental, Campus Universitario Las Lagunillas, 23071 Jaén, Spain
*
Author to whom correspondence should be addressed.
Nutrients 2019, 11(2), 220; https://doi.org/10.3390/nu11020220
Received: 28 December 2018 / Revised: 14 January 2019 / Accepted: 17 January 2019 / Published: 22 January 2019
(This article belongs to the Special Issue Gluten-Free Diet)
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Abstract

The high global demand of wheat and its subsequent consumption arise from the physicochemical properties of bread dough and its contribution to the protein intake in the human diet. Gluten is the main structural complex of wheat proteins and subjects affected by celiac disease (CD) cannot tolerate gluten protein. Within gluten proteins, α-gliadins constitute the most immunogenic fraction since they contain the main T-cell stimulating epitopes (DQ2.5-glia-α1, DQ2.5-glia-α2, and DQ2.5-glia-α3). In this work, the celiac immunotoxic potential of α-gliadins was studied within Triticeae: diploid, tetraploid, and hexaploid species. The abundance and immunostimulatory capacity of CD canonical epitopes and variants (with one or two mismatches) in all α-gliadin sequences were determined. The results showed that the canonical epitopes DQ2.5-glia-α1 and DQ2.5-glia-α3 were more frequent than DQ2.5-glia-α2. A higher abundance of canonical DQ2.5-glia-α1 epitope was found to be associated with genomes of the BBAADD, AA, and DD types; however, the abundance of DQ2.5-glia-α3 epitope variants was very high in BBAADD and BBAA wheat despite their low abundance in the canonical epitope. The most abundant substitution was that of proline to serine, which was disposed mainly on the three canonical DQ2.5 domains on position 8. Interestingly, our results demonstrated that the natural introduction of Q to H at any position eliminates the toxicity of the three T-cell epitopes in the α-gliadins. The results provided a rational approach for the introduction of natural amino acid substitutions to eliminate the toxicity of three T-cell epitopes, while maintaining the technological properties of commercial wheats. View Full-Text
Keywords: celiac disease; α-gliadin; 33-mer; DQ2.5-glia-α1; DQ2.5-glia-α2; DQ2.5-glia-α3 epitopes; wheat species celiac disease; α-gliadin; 33-mer; DQ2.5-glia-α1; DQ2.5-glia-α2; DQ2.5-glia-α3 epitopes; wheat species
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Ruiz-Carnicer, Á.; Comino, I.; Segura, V.; Ozuna, C.V.; Moreno, M.L.; López-Casado, M.Á.; Torres, M.I.; Barro, F.; Sousa, C. Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species. Nutrients 2019, 11, 220.

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