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: 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
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/83432
Acceso en línea:https://hdl.handle.net/11441/83432
https://doi.org/10.3390/nu11020220
Access Level:acceso abierto
Palabra clave: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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repository_id_str
spelling Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops SpeciesRuiz Carnicer, ÁngelaComino Montilla, Isabel MaríaSegura Montero, VerónicaOzuna Serafini, Carmen VictoriaMoreno Amador, María de LourdesLópez Casado, Miguel ÁngelTorres López, María IsabelBarro Losada, FranciscoSousa Martín, Carolinaceliac diseaseα-gliadin33-merDQ2.5-glia-α1DQ2.5-glia-α2DQ2.5-glia-α3epitopeswheat speciesThe 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.MDPIMicrobiología y Parasitología2019info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/83432https://doi.org/10.3390/nu11020220reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésNutrients, 11 (2), 220.https://doi.org/10.3390/nu11020220info:eu-repo/semantics/openAccessoai:idus.us.es:11441/834322026-06-17T12:51:07Z
dc.title.none.fl_str_mv 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
spellingShingle Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
Ruiz Carnicer, Ángela
celiac disease
α-gliadin
33-mer
DQ2.5-glia-α1
DQ2.5-glia-α2
DQ2.5-glia-α3
epitopes
wheat species
title_short 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_sort Celiac Immunogenic Potential of α-Gliadin Epitope Variants from Triticum and Aegilops Species
dc.creator.none.fl_str_mv 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
author Ruiz Carnicer, Ángela
author_facet 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
author_role author
author2 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
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Microbiología y Parasitología
dc.subject.none.fl_str_mv celiac disease
α-gliadin
33-mer
DQ2.5-glia-α1
DQ2.5-glia-α2
DQ2.5-glia-α3
epitopes
wheat species
topic celiac disease
α-gliadin
33-mer
DQ2.5-glia-α1
DQ2.5-glia-α2
DQ2.5-glia-α3
epitopes
wheat species
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.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/83432
https://doi.org/10.3390/nu11020220
url https://hdl.handle.net/11441/83432
https://doi.org/10.3390/nu11020220
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Nutrients, 11 (2), 220.
https://doi.org/10.3390/nu11020220
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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