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Abrogation of Immunogenic Properties of Gliadin Peptides through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor Dependent
[Image: see text] Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients with celiac disease. Transamidation of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten;...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5579586/ https://www.ncbi.nlm.nih.gov/pubmed/28771001 http://dx.doi.org/10.1021/acs.jafc.7b02557 |
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author | Zhou, Lin Kooy-Winkelaar, Yvonne M. C. Cordfunke, Robert A. Dragan, Irina Thompson, Allan Drijfhout, Jan Wouter van Veelen, Peter A. Chen, Hongbing Koning, Frits |
author_facet | Zhou, Lin Kooy-Winkelaar, Yvonne M. C. Cordfunke, Robert A. Dragan, Irina Thompson, Allan Drijfhout, Jan Wouter van Veelen, Peter A. Chen, Hongbing Koning, Frits |
author_sort | Zhou, Lin |
collection | PubMed |
description | [Image: see text] Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients with celiac disease. Transamidation of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten; however, little information is available on the minimal modification sufficient to eliminate gliadin immunogenicity nor has the effectiveness of transamidation been studied with T-cell clones from patients. Here we demonstrate that mTG can efficiently couple three different acyl-acceptor molecules, l-lysine, glycine ethyl ester, and hydroxylamine, to gliadin peptides and protein. While all three acyl-acceptor molecules were cross-linked to the same Q-residues, not all modifications were equally effective in silencing T-cell reactivity. Finally, we observed that tTG can partially reverse the mTG-catalyzed transamidation by its isopeptidase activity. These results set the stage to determine the impact of these modifications on the baking quality of gluten proteins and in vivo immunogenicity of such food products. |
format | Online Article Text |
id | pubmed-5579586 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-55795862017-09-05 Abrogation of Immunogenic Properties of Gliadin Peptides through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor Dependent Zhou, Lin Kooy-Winkelaar, Yvonne M. C. Cordfunke, Robert A. Dragan, Irina Thompson, Allan Drijfhout, Jan Wouter van Veelen, Peter A. Chen, Hongbing Koning, Frits J Agric Food Chem [Image: see text] Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients with celiac disease. Transamidation of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten; however, little information is available on the minimal modification sufficient to eliminate gliadin immunogenicity nor has the effectiveness of transamidation been studied with T-cell clones from patients. Here we demonstrate that mTG can efficiently couple three different acyl-acceptor molecules, l-lysine, glycine ethyl ester, and hydroxylamine, to gliadin peptides and protein. While all three acyl-acceptor molecules were cross-linked to the same Q-residues, not all modifications were equally effective in silencing T-cell reactivity. Finally, we observed that tTG can partially reverse the mTG-catalyzed transamidation by its isopeptidase activity. These results set the stage to determine the impact of these modifications on the baking quality of gluten proteins and in vivo immunogenicity of such food products. American Chemical Society 2017-08-03 2017-08-30 /pmc/articles/PMC5579586/ /pubmed/28771001 http://dx.doi.org/10.1021/acs.jafc.7b02557 Text en Copyright © 2017 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | Zhou, Lin Kooy-Winkelaar, Yvonne M. C. Cordfunke, Robert A. Dragan, Irina Thompson, Allan Drijfhout, Jan Wouter van Veelen, Peter A. Chen, Hongbing Koning, Frits Abrogation of Immunogenic Properties of Gliadin Peptides through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor Dependent |
title | Abrogation of Immunogenic Properties of Gliadin Peptides
through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor
Dependent |
title_full | Abrogation of Immunogenic Properties of Gliadin Peptides
through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor
Dependent |
title_fullStr | Abrogation of Immunogenic Properties of Gliadin Peptides
through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor
Dependent |
title_full_unstemmed | Abrogation of Immunogenic Properties of Gliadin Peptides
through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor
Dependent |
title_short | Abrogation of Immunogenic Properties of Gliadin Peptides
through Transamidation by Microbial Transglutaminase Is Acyl-Acceptor
Dependent |
title_sort | abrogation of immunogenic properties of gliadin peptides
through transamidation by microbial transglutaminase is acyl-acceptor
dependent |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5579586/ https://www.ncbi.nlm.nih.gov/pubmed/28771001 http://dx.doi.org/10.1021/acs.jafc.7b02557 |
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