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Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut

BACKGROUND: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from p...

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Autores principales: Vissers, Yvonne M., Blanc, Fany, Skov, Per Stahl, Johnson, Phil E., Rigby, Neil M., Przybylski-Nicaise, Laetitia, Bernard, Hervé, Wal, Jean-Michel, Ballmer-Weber, Barbara, Zuidmeer-Jongejan, Laurian, Szépfalusi, Zsolt, Ruinemans-Koerts, Janneke, Jansen, Ad P. H., Savelkoul, Huub F. J., Wichers, Harry J., Mackie, Alan R., Mills, Clare E. N., Adel-Patient, Karine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162016/
https://www.ncbi.nlm.nih.gov/pubmed/21901150
http://dx.doi.org/10.1371/journal.pone.0023998
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author Vissers, Yvonne M.
Blanc, Fany
Skov, Per Stahl
Johnson, Phil E.
Rigby, Neil M.
Przybylski-Nicaise, Laetitia
Bernard, Hervé
Wal, Jean-Michel
Ballmer-Weber, Barbara
Zuidmeer-Jongejan, Laurian
Szépfalusi, Zsolt
Ruinemans-Koerts, Janneke
Jansen, Ad P. H.
Savelkoul, Huub F. J.
Wichers, Harry J.
Mackie, Alan R.
Mills, Clare E. N.
Adel-Patient, Karine
author_facet Vissers, Yvonne M.
Blanc, Fany
Skov, Per Stahl
Johnson, Phil E.
Rigby, Neil M.
Przybylski-Nicaise, Laetitia
Bernard, Hervé
Wal, Jean-Michel
Ballmer-Weber, Barbara
Zuidmeer-Jongejan, Laurian
Szépfalusi, Zsolt
Ruinemans-Koerts, Janneke
Jansen, Ad P. H.
Savelkoul, Huub F. J.
Wichers, Harry J.
Mackie, Alan R.
Mills, Clare E. N.
Adel-Patient, Karine
author_sort Vissers, Yvonne M.
collection PubMed
description BACKGROUND: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. METHODOLOGY/PRINCIPAL FINDINGS: Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. CONCLUSIONS/SIGNIFICANCE: Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.
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spelling pubmed-31620162011-09-07 Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut Vissers, Yvonne M. Blanc, Fany Skov, Per Stahl Johnson, Phil E. Rigby, Neil M. Przybylski-Nicaise, Laetitia Bernard, Hervé Wal, Jean-Michel Ballmer-Weber, Barbara Zuidmeer-Jongejan, Laurian Szépfalusi, Zsolt Ruinemans-Koerts, Janneke Jansen, Ad P. H. Savelkoul, Huub F. J. Wichers, Harry J. Mackie, Alan R. Mills, Clare E. N. Adel-Patient, Karine PLoS One Research Article BACKGROUND: Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. METHODOLOGY/PRINCIPAL FINDINGS: Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. CONCLUSIONS/SIGNIFICANCE: Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins. Public Library of Science 2011-08-25 /pmc/articles/PMC3162016/ /pubmed/21901150 http://dx.doi.org/10.1371/journal.pone.0023998 Text en Vissers et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Vissers, Yvonne M.
Blanc, Fany
Skov, Per Stahl
Johnson, Phil E.
Rigby, Neil M.
Przybylski-Nicaise, Laetitia
Bernard, Hervé
Wal, Jean-Michel
Ballmer-Weber, Barbara
Zuidmeer-Jongejan, Laurian
Szépfalusi, Zsolt
Ruinemans-Koerts, Janneke
Jansen, Ad P. H.
Savelkoul, Huub F. J.
Wichers, Harry J.
Mackie, Alan R.
Mills, Clare E. N.
Adel-Patient, Karine
Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
title Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
title_full Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
title_fullStr Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
title_full_unstemmed Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
title_short Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
title_sort effect of heating and glycation on the allergenicity of 2s albumins (ara h 2/6) from peanut
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162016/
https://www.ncbi.nlm.nih.gov/pubmed/21901150
http://dx.doi.org/10.1371/journal.pone.0023998
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