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...

Full description

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-06-01
Series:Frontiers in Plant Science
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fpls.2018.00818/full
_version_ 1819156209832296448
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.
first_indexed 2024-12-22T15:49:14Z
format Article
id doaj.art-0e523ec27d954e04bc00143116689f0e
institution Directory Open Access Journal
issn 1664-462X
language English
last_indexed 2024-12-22T15:49:14Z
publishDate 2018-06-01
publisher Frontiers Media S.A.
record_format Article
series Frontiers in Plant Science
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
work_keys_str_mv AT kyoungwoncho proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT hyerangbeom proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT youranjang proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT susanbaltenbach proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT williamhvensel proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT annamariasimonbuss proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT sunhyunglim proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT mingkim proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat
AT jongyeollee proteomicprofilingandepitopeanalysisofthecomplexagandōgliadinfamiliesinacommercialbreadwheat