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Towards coeliac‐safe bread

Gluten‐free foods cannot substitute for products made from wheat flour. When wheat products are digested, the remaining peptides can trigger an autoimmune disease in 1% of the North American and European population, called coeliac disease. Because wheat proteins are encoded by a large gene family, i...

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Autores principales: Zhang, Zhiyong, Deng, Yiting, Zhang, Wei, Wu, Yongrui, Messing, Joachim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7061869/
https://www.ncbi.nlm.nih.gov/pubmed/31585498
http://dx.doi.org/10.1111/pbi.13273
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author Zhang, Zhiyong
Deng, Yiting
Zhang, Wei
Wu, Yongrui
Messing, Joachim
author_facet Zhang, Zhiyong
Deng, Yiting
Zhang, Wei
Wu, Yongrui
Messing, Joachim
author_sort Zhang, Zhiyong
collection PubMed
description Gluten‐free foods cannot substitute for products made from wheat flour. When wheat products are digested, the remaining peptides can trigger an autoimmune disease in 1% of the North American and European population, called coeliac disease. Because wheat proteins are encoded by a large gene family, it has been impossible to use conventional breeding to select wheat varieties that are coeliac‐safe. However, one can test the properties of protein variants by expressing single genes in coeliac‐safe cereals like maize. One source of protein that can be considered as coeliac‐safe and has bread‐making properties is teff (Eragrostis tef), a grain consumed in Ethiopia. Here, we show that teff α‐globulin3 (Etglo3) forms storage vacuoles in maize that are morphologically similar to those of wheat. Using transmission electron microscopy, immunogold labelling shows that Etglo3 is almost exclusively deposited in the storage vacuole as electron‐dense aggregates. Of maize seed storage proteins, 27‐kDa γ‐zein is co‐deposited with Etglo3. Etglo3 polymerizes via intermolecular disulphide bonds in maize, similar to wheat HMW glutenins under non‐reducing conditions. Crossing maize Etglo3 transgenic lines with α‐, β‐ and γ‐zein RNA interference (RNAi) lines reveals that Etglo3 accumulation is only dramatically reduced in γ‐zein RNAi background. This suggests that Etglo3 and 27‐kDa γ‐zein together cause storage vacuole formation and behave similar to the interactions of glutenins and gliadins in wheat. Therefore, expression of teff α‐globulins in maize presents a major step in the development of a coeliac‐safe grain with bread‐making properties.
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spelling pubmed-70618692020-03-16 Towards coeliac‐safe bread Zhang, Zhiyong Deng, Yiting Zhang, Wei Wu, Yongrui Messing, Joachim Plant Biotechnol J Research Articles Gluten‐free foods cannot substitute for products made from wheat flour. When wheat products are digested, the remaining peptides can trigger an autoimmune disease in 1% of the North American and European population, called coeliac disease. Because wheat proteins are encoded by a large gene family, it has been impossible to use conventional breeding to select wheat varieties that are coeliac‐safe. However, one can test the properties of protein variants by expressing single genes in coeliac‐safe cereals like maize. One source of protein that can be considered as coeliac‐safe and has bread‐making properties is teff (Eragrostis tef), a grain consumed in Ethiopia. Here, we show that teff α‐globulin3 (Etglo3) forms storage vacuoles in maize that are morphologically similar to those of wheat. Using transmission electron microscopy, immunogold labelling shows that Etglo3 is almost exclusively deposited in the storage vacuole as electron‐dense aggregates. Of maize seed storage proteins, 27‐kDa γ‐zein is co‐deposited with Etglo3. Etglo3 polymerizes via intermolecular disulphide bonds in maize, similar to wheat HMW glutenins under non‐reducing conditions. Crossing maize Etglo3 transgenic lines with α‐, β‐ and γ‐zein RNA interference (RNAi) lines reveals that Etglo3 accumulation is only dramatically reduced in γ‐zein RNAi background. This suggests that Etglo3 and 27‐kDa γ‐zein together cause storage vacuole formation and behave similar to the interactions of glutenins and gliadins in wheat. Therefore, expression of teff α‐globulins in maize presents a major step in the development of a coeliac‐safe grain with bread‐making properties. John Wiley and Sons Inc. 2019-12-24 2020-04 /pmc/articles/PMC7061869/ /pubmed/31585498 http://dx.doi.org/10.1111/pbi.13273 Text en © 2019 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Zhang, Zhiyong
Deng, Yiting
Zhang, Wei
Wu, Yongrui
Messing, Joachim
Towards coeliac‐safe bread
title Towards coeliac‐safe bread
title_full Towards coeliac‐safe bread
title_fullStr Towards coeliac‐safe bread
title_full_unstemmed Towards coeliac‐safe bread
title_short Towards coeliac‐safe bread
title_sort towards coeliac‐safe bread
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7061869/
https://www.ncbi.nlm.nih.gov/pubmed/31585498
http://dx.doi.org/10.1111/pbi.13273
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