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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Online Access: | http://hdl.handle.net/10261/130632 https://doi.org/10.4414/smw.2015.14128 |
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ftcsic:oai:digital.csic.es:10261/130632 2024-02-11T10:01:59+01:00 Fish β-parvalbumin acquires allergenic properties by amyloid assembly Martínez, Javier Sánchez, Rosa Castellanos, Milagros Fernández-Escamilla, A. M. Vázquez-Cortés, S. Fernández-Rivas, M. Gasset, M. 2015 http://hdl.handle.net/10261/130632 https://doi.org/10.4414/smw.2015.14128 unknown EMH Swiss Medical Publishers Publisher's version Sí doi:10.4414/smw.2015.14128 issn: 1424-3997 Swiss Medical Weekly 145 (2015) http://hdl.handle.net/10261/130632 open artículo http://purl.org/coar/resource_type/c_6501 2015 ftcsic https://doi.org/10.4414/smw.2015.14128 2024-01-16T10:14:34Z 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. Peer Reviewed Article in Journal/Newspaper atlantic cod Digital.CSIC (Spanish National Research Council) Swiss Medical Weekly |
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Digital.CSIC (Spanish National Research Council) |
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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. Peer Reviewed |
format |
Article in Journal/Newspaper |
author |
Martínez, Javier Sánchez, Rosa Castellanos, Milagros Fernández-Escamilla, A. M. Vázquez-Cortés, S. Fernández-Rivas, M. Gasset, M. |
spellingShingle |
Martínez, Javier Sánchez, Rosa Castellanos, Milagros Fernández-Escamilla, A. M. Vázquez-Cortés, S. Fernández-Rivas, M. Gasset, M. Fish β-parvalbumin acquires allergenic properties by amyloid assembly |
author_facet |
Martínez, Javier Sánchez, Rosa Castellanos, Milagros Fernández-Escamilla, A. M. Vázquez-Cortés, S. Fernández-Rivas, M. Gasset, M. |
author_sort |
Martínez, Javier |
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 |
EMH Swiss Medical Publishers |
publishDate |
2015 |
url |
http://hdl.handle.net/10261/130632 https://doi.org/10.4414/smw.2015.14128 |
genre |
atlantic cod |
genre_facet |
atlantic cod |
op_relation |
Publisher's version Sí doi:10.4414/smw.2015.14128 issn: 1424-3997 Swiss Medical Weekly 145 (2015) http://hdl.handle.net/10261/130632 |
op_rights |
open |
op_doi |
https://doi.org/10.4414/smw.2015.14128 |
container_title |
Swiss Medical Weekly |
_version_ |
1790597874962137088 |