ArticleProtein science : a publication of the Protein Society2024
Comparative studies of seafood and reptile α- and β-parvalbumins.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Peptidomimetic Modified Heptamethine Cyanine Dyes for Enhanced Bioimaging Targetability: A Molecular Interaction Study on Bovine Serum Albumin and Human Parvalbumin.Journal of medicinal chemistry · 2026Article
- 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
- Calcium-binding proteins as allergens.Frontiers in allergy · 2026Review
- Fish isoallergens and variants: database compilation,Frontiers in bioinformatics · 2025Article
- Comparative studies of seafood and reptile α- and β-parvalbumins.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
9 authors.
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Abstract
Small calcium-binding proteins such as parvalbumins (PVs) are major seafood and fish allergens. However, the impact of structural changes on their capacity to bind IgE has not been studied in detail. Therefore, fish and reptilian PVs, as well as human α-PV, were selected for biochemical, structural, and IgE binding studies. Likely due to their high solubility, crystallization proved difficult, so additional techniques were used to promote crystallization of the proteins. Novel crystal structures were determined for human PV, cod allergen Gad m 1.0201, saltwater crocodile allergen Cro p 1.0101, and the α-PV from thornback ray. β-PVs are considered the major fish allergens, while α-PVs are rarely categorized as allergens. To explain these differences, the results of structural and IgE binding studies were combined. This approach allowed us to provide new insight into IgE binding epitopes present on PVs, focusing on cross-reactivity among the selected α- and β-PVs. In addition, we have shown that these proteins display remarkable thermal stability across a range of pH conditions, which is relevant in the case of food allergens and food processing. Moreover, it is shown that the presence of calcium cations is critical for stability of the studied PVs via their protein folding, which has an impact on the formation of IgE binding epitopes. These studies shows the stability of fish and reptile PV allergens, and it allows for further evaluation of their IgE cross-reactivity.
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