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

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 g...

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Autores principales: Ruiz-Carnicer, Ángela, Comino, Isabel, Segura, Verónica, Ozuna, Carmen V., Moreno, María de Lourdes, López-Casado, Miguel Ángel, Torres, María Isabel, Barro, Francisco, Sousa, Carolina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6413208/
https://www.ncbi.nlm.nih.gov/pubmed/30678169
http://dx.doi.org/10.3390/nu11020220
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author Ruiz-Carnicer, Ángela
Comino, Isabel
Segura, Verónica
Ozuna, Carmen V.
Moreno, María de Lourdes
López-Casado, Miguel Ángel
Torres, María Isabel
Barro, Francisco
Sousa, Carolina
author_facet Ruiz-Carnicer, Ángela
Comino, Isabel
Segura, Verónica
Ozuna, Carmen V.
Moreno, María de Lourdes
López-Casado, Miguel Ángel
Torres, María Isabel
Barro, Francisco
Sousa, Carolina
author_sort Ruiz-Carnicer, Ángela
collection PubMed
description 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.
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spelling pubmed-64132082019-03-29 Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species Ruiz-Carnicer, Ángela Comino, Isabel Segura, Verónica Ozuna, Carmen V. Moreno, María de Lourdes López-Casado, Miguel Ángel Torres, María Isabel Barro, Francisco Sousa, Carolina Nutrients Article 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. MDPI 2019-01-22 /pmc/articles/PMC6413208/ /pubmed/30678169 http://dx.doi.org/10.3390/nu11020220 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ruiz-Carnicer, Ángela
Comino, Isabel
Segura, Verónica
Ozuna, Carmen V.
Moreno, María de Lourdes
López-Casado, Miguel Ángel
Torres, María Isabel
Barro, Francisco
Sousa, Carolina
Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
title Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
title_full Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
title_fullStr Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
title_full_unstemmed Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
title_short Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
title_sort celiac immunogenic potential of α-gliadin epitope variants from triticum and aegilops species
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6413208/
https://www.ncbi.nlm.nih.gov/pubmed/30678169
http://dx.doi.org/10.3390/nu11020220
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