Artículo
Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
Autor/es | Ruiz Carnicer, Ángela
Comino Montilla, Isabel María Segura Montero, Verónica Ozuna Serafini, Carmen Victoria Moreno Amador, María de Lourdes López Casado, Miguel Ángel Torres López, María Isabel Barro Losada, Francisco Sousa Martín, Carolina |
Departamento | Universidad de Sevilla. Departamento de Microbiología y Parasitología |
Fecha de publicación | 2019-01 |
Fecha de depósito | 2019-02-25 |
Publicado en |
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Resumen | 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 ... 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. |
Cita | Ruiz Carnicer, Á., Comino Montilla, I.M., Segura Montero, V., Ozuna Serafini, C.V., Moreno Amador, M.d.L., López Casado, M.Á.,...,Sousa Martín, C. (2019). Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species. Nutrients, 11 (2), 220. |
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