Fish β-parvalbumin acquires allergenic properties by amyloid assembly
PRINCIPLES: Amyloids are highly cross-β-sheet-rich aggregated states that confer protease resistance, membrane activity and multivalence properties to proteins, all essential features for the undesired preservation of food proteins transiting the gastrointestinal tract and causing type I allergy. ME...
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ftdoajarticles:oai:doaj.org/article:b97d81dfad394b739dcd9c3a27937b95 2023-05-15T15:27:38+02:00 Fish β-parvalbumin acquires allergenic properties by amyloid assembly Javier Martínez Rosa Sánchez Milagros Castellanos Ana M Fernández-Escamilla Sonia Vazquez-Cortés Montserrat Fernández-Rivas Maria Gasset 2015-05-01T00:00:00Z https://doi.org/10.4414/smw.2015.14128 https://doaj.org/article/b97d81dfad394b739dcd9c3a27937b95 EN eng SMW supporting association (Trägerverein Swiss Medical Weekly SMW) https://www.smw.ch/index.php/smw/article/view/2030 https://doaj.org/toc/1424-3997 doi:10.4414/smw.2015.14128 1424-3997 https://doaj.org/article/b97d81dfad394b739dcd9c3a27937b95 Swiss Medical Weekly, Vol 145, Iss 2122 (2015) type I food allergy fish allergens fish β-parvalbumin amyloids Medicine R article 2015 ftdoajarticles https://doi.org/10.4414/smw.2015.14128 2022-12-30T20:51:32Z PRINCIPLES: Amyloids are highly cross-β-sheet-rich aggregated states that confer protease resistance, membrane activity and multivalence properties to proteins, all essential features for the undesired preservation of food proteins transiting the gastrointestinal tract and causing type I allergy. METHODS: Amyloid propensity of β-parvalbumin, the major fish allergen, was theoretically analysed and assayed under gastrointestinal-relevant conditions using the binding of thioflavin T, the formation of sodium dodecyl sulphate- (SDS-) resistant aggregates, circular dichroism spectroscopy and atomic force microscopy fibril imaging. Impact of amyloid aggregates on allergenicity was assessed with dot blot. RESULTS: Sequences of β-parvalbumin from species with commercial value contain several adhesive hexapeptides capable of driving amyloid formation. Using Atlantic cod β-parvalbumin (rGad m 1) displaying high IgE cross-reactivity, we found that formation of amyloid fibres under simulated gastrointestinal conditions accounts for the resistance to acid and neutral proteases, for the presence of membrane active species under gastrointestinal relevant conditions and for the IgE-recognition in the sera of allergic patients. Incorporation of the anti-amyloid compound epigallocatechin gallate prevents rGad m 1 fibrillation, facilitates its protease digestion and impairs its recognition by IgE. CONCLUSIONS: the formation of amyloid by rGad m 1 explains its degradation resistance, its facilitated passage across the intestinal epithelial barrier and its epitope architecture as allergen. Article in Journal/Newspaper atlantic cod Directory of Open Access Journals: DOAJ Articles Swiss Medical Weekly |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
type I food allergy fish allergens fish β-parvalbumin amyloids Medicine R |
spellingShingle |
type I food allergy fish allergens fish β-parvalbumin amyloids Medicine R Javier Martínez Rosa Sánchez Milagros Castellanos Ana M Fernández-Escamilla Sonia Vazquez-Cortés Montserrat Fernández-Rivas Maria Gasset Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
topic_facet |
type I food allergy fish allergens fish β-parvalbumin amyloids Medicine R |
description |
PRINCIPLES: Amyloids are highly cross-β-sheet-rich aggregated states that confer protease resistance, membrane activity and multivalence properties to proteins, all essential features for the undesired preservation of food proteins transiting the gastrointestinal tract and causing type I allergy. METHODS: Amyloid propensity of β-parvalbumin, the major fish allergen, was theoretically analysed and assayed under gastrointestinal-relevant conditions using the binding of thioflavin T, the formation of sodium dodecyl sulphate- (SDS-) resistant aggregates, circular dichroism spectroscopy and atomic force microscopy fibril imaging. Impact of amyloid aggregates on allergenicity was assessed with dot blot. RESULTS: Sequences of β-parvalbumin from species with commercial value contain several adhesive hexapeptides capable of driving amyloid formation. Using Atlantic cod β-parvalbumin (rGad m 1) displaying high IgE cross-reactivity, we found that formation of amyloid fibres under simulated gastrointestinal conditions accounts for the resistance to acid and neutral proteases, for the presence of membrane active species under gastrointestinal relevant conditions and for the IgE-recognition in the sera of allergic patients. Incorporation of the anti-amyloid compound epigallocatechin gallate prevents rGad m 1 fibrillation, facilitates its protease digestion and impairs its recognition by IgE. CONCLUSIONS: the formation of amyloid by rGad m 1 explains its degradation resistance, its facilitated passage across the intestinal epithelial barrier and its epitope architecture as allergen. |
format |
Article in Journal/Newspaper |
author |
Javier Martínez Rosa Sánchez Milagros Castellanos Ana M Fernández-Escamilla Sonia Vazquez-Cortés Montserrat Fernández-Rivas Maria Gasset |
author_facet |
Javier Martínez Rosa Sánchez Milagros Castellanos Ana M Fernández-Escamilla Sonia Vazquez-Cortés Montserrat Fernández-Rivas Maria Gasset |
author_sort |
Javier Martínez |
title |
Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
title_short |
Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
title_full |
Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
title_fullStr |
Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
title_full_unstemmed |
Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
title_sort |
fish β-parvalbumin acquires allergenic properties by amyloid assembly |
publisher |
SMW supporting association (Trägerverein Swiss Medical Weekly SMW) |
publishDate |
2015 |
url |
https://doi.org/10.4414/smw.2015.14128 https://doaj.org/article/b97d81dfad394b739dcd9c3a27937b95 |
genre |
atlantic cod |
genre_facet |
atlantic cod |
op_source |
Swiss Medical Weekly, Vol 145, Iss 2122 (2015) |
op_relation |
https://www.smw.ch/index.php/smw/article/view/2030 https://doaj.org/toc/1424-3997 doi:10.4414/smw.2015.14128 1424-3997 https://doaj.org/article/b97d81dfad394b739dcd9c3a27937b95 |
op_doi |
https://doi.org/10.4414/smw.2015.14128 |
container_title |
Swiss Medical Weekly |
_version_ |
1766358064336732160 |