Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat
Wheat gliadins are a complex group of proteins that contribute to the functional properties of wheat flour doughs and contain epitopes that are relevant for celiac disease (CD) and wheat-dependent exercise-induced anaphylaxis (WDEIA). In this study, we extracted ethanol-soluble gliadin fractions fro...
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Frontiers Media S.A.
2018-06-01
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Online Access: | https://www.frontiersin.org/article/10.3389/fpls.2018.00818/full |
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author | Kyoungwon Cho Hye-Rang Beom You-Ran Jang Susan B. Altenbach William H. Vensel Annamaria Simon-Buss Sun-Hyung Lim Min G. Kim Jong-Yeol Lee |
author_facet | Kyoungwon Cho Hye-Rang Beom You-Ran Jang Susan B. Altenbach William H. Vensel Annamaria Simon-Buss Sun-Hyung Lim Min G. Kim Jong-Yeol Lee |
author_sort | Kyoungwon Cho |
collection | DOAJ |
description | Wheat gliadins are a complex group of proteins that contribute to the functional properties of wheat flour doughs and contain epitopes that are relevant for celiac disease (CD) and wheat-dependent exercise-induced anaphylaxis (WDEIA). In this study, we extracted ethanol-soluble gliadin fractions from flour of the Korean bread wheat cultivar Keumkang. Proteins were separated by 2-dimensional gel electrophoresis (2-DE) using a pI range of 6–11 in the first dimension and subjected to tandem mass spectrometry. α-, γ-, and ω-gliadins were identified as the predominant proteins in 31, 28, and one 2-DE spot, respectively. An additional six ω-gliadins were identified in a separate experiment in which a pI range of 3–11 was used for protein separation. We analyzed the composition of CD- and WDEIA-relevant epitopes in the gliadin sequences from Keumkang flour, demonstrating the immunogenic potential of this cultivar. Detailed knowledge about the complement of gliadins accumulated in Keumkang flour provides the background necessary to devise either breeding or biotechnology strategies to improve the functional properties and reduce the adverse health effects of the flour. |
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language | English |
last_indexed | 2024-12-22T15:49:14Z |
publishDate | 2018-06-01 |
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spelling | doaj.art-0e523ec27d954e04bc00143116689f0e2022-12-21T18:20:56ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2018-06-01910.3389/fpls.2018.00818354819Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread WheatKyoungwon Cho0Hye-Rang Beom1You-Ran Jang2Susan B. Altenbach3William H. Vensel4Annamaria Simon-Buss5Sun-Hyung Lim6Min G. Kim7Jong-Yeol Lee8National Institute of Agricultural Sciences, Rural Development Administration, Jeonju, South KoreaNational Institute of Agricultural Sciences, Rural Development Administration, Jeonju, South KoreaNational Institute of Agricultural Sciences, Rural Development Administration, Jeonju, South KoreaWestern Regional Research Center, United States Department of Agriculture, Agricultural Research Service, Albany, CA, United StatesWestern Regional Research Center, United States Department of Agriculture, Agricultural Research Service, Albany, CA, United StatesWestern Regional Research Center, United States Department of Agriculture, Agricultural Research Service, Albany, CA, United StatesNational Institute of Agricultural Sciences, Rural Development Administration, Jeonju, South KoreaCollege of Pharmacy and Research Institute of Pharmaceutical Science, Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, South KoreaNational Institute of Agricultural Sciences, Rural Development Administration, Jeonju, South KoreaWheat gliadins are a complex group of proteins that contribute to the functional properties of wheat flour doughs and contain epitopes that are relevant for celiac disease (CD) and wheat-dependent exercise-induced anaphylaxis (WDEIA). In this study, we extracted ethanol-soluble gliadin fractions from flour of the Korean bread wheat cultivar Keumkang. Proteins were separated by 2-dimensional gel electrophoresis (2-DE) using a pI range of 6–11 in the first dimension and subjected to tandem mass spectrometry. α-, γ-, and ω-gliadins were identified as the predominant proteins in 31, 28, and one 2-DE spot, respectively. An additional six ω-gliadins were identified in a separate experiment in which a pI range of 3–11 was used for protein separation. We analyzed the composition of CD- and WDEIA-relevant epitopes in the gliadin sequences from Keumkang flour, demonstrating the immunogenic potential of this cultivar. Detailed knowledge about the complement of gliadins accumulated in Keumkang flour provides the background necessary to devise either breeding or biotechnology strategies to improve the functional properties and reduce the adverse health effects of the flour.https://www.frontiersin.org/article/10.3389/fpls.2018.00818/fullgliadinsproteomic profilingepitope analysisceliac diseasefood allergy |
spellingShingle | Kyoungwon Cho Hye-Rang Beom You-Ran Jang Susan B. Altenbach William H. Vensel Annamaria Simon-Buss Sun-Hyung Lim Min G. Kim Jong-Yeol Lee Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat Frontiers in Plant Science gliadins proteomic profiling epitope analysis celiac disease food allergy |
title | Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat |
title_full | Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat |
title_fullStr | Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat |
title_full_unstemmed | Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat |
title_short | Proteomic Profiling and Epitope Analysis of the Complex α-, γ-, and ω-Gliadin Families in a Commercial Bread Wheat |
title_sort | proteomic profiling and epitope analysis of the complex α γ and ω gliadin families in a commercial bread wheat |
topic | gliadins proteomic profiling epitope analysis celiac disease food allergy |
url | https://www.frontiersin.org/article/10.3389/fpls.2018.00818/full |
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