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Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease
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 th...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209737/ https://www.ncbi.nlm.nih.gov/pubmed/28051174 http://dx.doi.org/10.1038/srep39876 |
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author | Gell, Gyöngyvér Kovács, Krisztina Veres, Gábor Korponay-Szabó, Ilma R. Juhász, Angéla |
author_facet | Gell, Gyöngyvér Kovács, Krisztina Veres, Gábor Korponay-Szabó, Ilma R. Juhász, Angéla |
author_sort | Gell, Gyöngyvér |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5209737 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-52097372017-01-05 Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease Gell, Gyöngyvér Kovács, Krisztina Veres, Gábor Korponay-Szabó, Ilma R. Juhász, Angéla Sci Rep Article 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. Nature Publishing Group 2017-01-04 /pmc/articles/PMC5209737/ /pubmed/28051174 http://dx.doi.org/10.1038/srep39876 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Gell, Gyöngyvér Kovács, Krisztina Veres, Gábor Korponay-Szabó, Ilma R. Juhász, Angéla Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
title | Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
title_full | Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
title_fullStr | Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
title_full_unstemmed | Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
title_short | Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
title_sort | characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209737/ https://www.ncbi.nlm.nih.gov/pubmed/28051174 http://dx.doi.org/10.1038/srep39876 |
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