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Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition

The effect of glycation and aggregation of thermally processed β-lactoglobulin (BLG) on binding to sRAGE and specific immunoglobulin E (sIgE) from cow milk allergic (CMA) patients were investigated. BLG was heated under dry conditions (water activity < 0.7) and wet conditions (in phosphate buffer...

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Autores principales: Zenker, Hannah E., Ewaz, Arifa, Deng, Ying, Savelkoul, Huub F. J., van Neerven, R.J. Joost, De Jong, Nicolette W., Wichers, Harry J., Hettinga, Kasper A., Teodorowicz, Malgorzata
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627217/
https://www.ncbi.nlm.nih.gov/pubmed/31242665
http://dx.doi.org/10.3390/nu11061432
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author Zenker, Hannah E.
Ewaz, Arifa
Deng, Ying
Savelkoul, Huub F. J.
van Neerven, R.J. Joost
De Jong, Nicolette W.
Wichers, Harry J.
Hettinga, Kasper A.
Teodorowicz, Malgorzata
author_facet Zenker, Hannah E.
Ewaz, Arifa
Deng, Ying
Savelkoul, Huub F. J.
van Neerven, R.J. Joost
De Jong, Nicolette W.
Wichers, Harry J.
Hettinga, Kasper A.
Teodorowicz, Malgorzata
author_sort Zenker, Hannah E.
collection PubMed
description The effect of glycation and aggregation of thermally processed β-lactoglobulin (BLG) on binding to sRAGE and specific immunoglobulin E (sIgE) from cow milk allergic (CMA) patients were investigated. BLG was heated under dry conditions (water activity < 0.7) and wet conditions (in phosphate buffer at pH 7.4) at low temperature (<73 °C) and high temperatures (>90 °C) in the presence or absence of the milk sugar lactose. Nε-(carboxymethyl)-l-lysine (CML) western blot and glycation staining were used to directly identify glycation structures on the protein fractions on SDS-PAGE. Western blot was used to specify sRAGE and sIgE binding fractions. sRAGE binding was highest under wet-heated BLG independent of the presence of the milk sugar lactose. Under wet heating, high-molecular-weight aggregates were most potent and did not require the presence of CML to generate sRAGE binding ligands. In the dry system, sRAGE binding was observed only in the presence of lactose. sIgE binding affinity showed large individual differences and revealed four binding profiles. Dependent on the individual, sIgE binding decreased or increased by wet heating independent of the presence of lactose. Dry heating required the presence of lactose to show increased binding to aggregates in most individuals. This study highlights an important role of heating condition-dependent protein aggregation and glycation in changing the immunogenicity and antigenicity of cow’s milk BLG.
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spelling pubmed-66272172019-07-23 Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition Zenker, Hannah E. Ewaz, Arifa Deng, Ying Savelkoul, Huub F. J. van Neerven, R.J. Joost De Jong, Nicolette W. Wichers, Harry J. Hettinga, Kasper A. Teodorowicz, Malgorzata Nutrients Article The effect of glycation and aggregation of thermally processed β-lactoglobulin (BLG) on binding to sRAGE and specific immunoglobulin E (sIgE) from cow milk allergic (CMA) patients were investigated. BLG was heated under dry conditions (water activity < 0.7) and wet conditions (in phosphate buffer at pH 7.4) at low temperature (<73 °C) and high temperatures (>90 °C) in the presence or absence of the milk sugar lactose. Nε-(carboxymethyl)-l-lysine (CML) western blot and glycation staining were used to directly identify glycation structures on the protein fractions on SDS-PAGE. Western blot was used to specify sRAGE and sIgE binding fractions. sRAGE binding was highest under wet-heated BLG independent of the presence of the milk sugar lactose. Under wet heating, high-molecular-weight aggregates were most potent and did not require the presence of CML to generate sRAGE binding ligands. In the dry system, sRAGE binding was observed only in the presence of lactose. sIgE binding affinity showed large individual differences and revealed four binding profiles. Dependent on the individual, sIgE binding decreased or increased by wet heating independent of the presence of lactose. Dry heating required the presence of lactose to show increased binding to aggregates in most individuals. This study highlights an important role of heating condition-dependent protein aggregation and glycation in changing the immunogenicity and antigenicity of cow’s milk BLG. MDPI 2019-06-25 /pmc/articles/PMC6627217/ /pubmed/31242665 http://dx.doi.org/10.3390/nu11061432 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zenker, Hannah E.
Ewaz, Arifa
Deng, Ying
Savelkoul, Huub F. J.
van Neerven, R.J. Joost
De Jong, Nicolette W.
Wichers, Harry J.
Hettinga, Kasper A.
Teodorowicz, Malgorzata
Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition
title Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition
title_full Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition
title_fullStr Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition
title_full_unstemmed Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition
title_short Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition
title_sort differential effects of dry vs. wet heating of β-lactoglobulin on formation of srage binding ligands and sige epitope recognition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627217/
https://www.ncbi.nlm.nih.gov/pubmed/31242665
http://dx.doi.org/10.3390/nu11061432
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