ArticleScientific reports2019
Reconstruction of fish allergenicity from the content and structural traits of the component β-parvalbumin isoforms.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Optimizing the Functional and Safety Properties of a Marine Allergen: Maillard-Induced Conjugation of Chitosan and Saccharides Attenuates the Allergenicity of Turbot (Foods (Basel, Switzerland) · 2026Article
- Molecular sensitization profiles and β-parvalbumin sensitization burden associated with clinical fish allergy in children.Frontiers in immunology · 2026Article
- Proteomic Characterization of Major Fish Allergy Responsive Protein Parvalbumins in Hilsa (Journal of agricultural and food chemistry · 2025Article
- Mass Spectrometry-Based Proteomics for Seafood Allergen Detection and Quantification: Current Trends and Technological Frontiers.International journal of molecular sciences · 2025Review
- Review
- Parvalbumin Gene: A Valuable Marker for Pike Authentication and Allergen Risk Assessment.Journal of agricultural and food chemistry · 2024Article
- Article
- Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species.Biology · 2022Article
- Fish Processing and Digestion Affect Parvalbumins Detectability in Gilthead Seabream and European Seabass.Animals : an open access journal from MDPI · 2022Article
- Fish Allergenicity Modulation Using Tailored Enriched Diets-Where Are We?Frontiers in physiology · 2022Review
- Fish Allergy Around the World-Precise Diagnosis to Facilitate Patient Management.Frontiers in allergy · 2021Review
- Proteomics-Based Methodologies for the Detection and Quantification of Seafood Allergens.Foods (Basel, Switzerland) · 2020Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most fish-allergic patients have anti-β-parvalbumin (β-PV) immunoglobulin E (IgE), which cross-reacts among fish species with variable clinical effects. Although the β-PV load is considered a determinant for allergenicity, fish species express distinct β-PV isoforms with unknown pathogenic contributions. To identify the role various parameters play in allergenicity, we have taken Gadus morhua and Scomber japonicus models, determined their β-PV isoform composition and analyzed the interaction of the IgE from fish-allergic patient sera with these different conformations. We found that each fish species contains a major and a minor isoform, with the total PV content four times higher in Gadus morhua than in Scomber japonicus. The isoforms showing the best IgE recognition displayed protease-sensitive globular folds, and if forming amyloids, they were not immunoreactive. Of the isoforms displaying stable globular folds, one was not recognized by IgE under any of the conditions, and the other formed highly immunoreactive amyloids. The results showed that Gadus morhua muscles are equipped with an isoform combination and content that ensures the IgE recognition of all PV folds, whereas the allergenic load of Scomber japonicus is under the control of proteolysis. We conclude that the consideration of isoform properties and content may improve the explanation of fish species allergenicity differences.
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