ArticleScientific reports2021
Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Genetic Polymorphisms of InvasivePlants (Basel, Switzerland) · 2025Article
- Human IgE monoclonal antibodies define two unusual epitopes trapping dog allergen Can f 1 in different conformations.Protein science : a publication of the Protein Society · 2025Article
- Conformational Flexibility of a Lipocalin Allergen (Mus m 1): Implications for Molecular Allergy Diagnostics.Current issues in molecular biology · 2025Article
- Update on hazelnut allergy: Allergen characterization, epidemiology, food processing technique and detecting strategy.Comprehensive reviews in food science and food safety · 2025Review
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- Allergenicity and structural properties of new Cor a 1 isoallergens from hazel identified in different plant tissues.Scientific reports · 2024Article
- Structural Characterization of Food Allergens by Nuclear Magnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen.Foods (Basel, Switzerland) · 2023Article
- The role of the DE and EF loop of BKPyV VP1 in the serological cross-reactivity between subtypes.Virus research · 2023Article
- Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1.Foods (Basel, Switzerland) · 2022Article
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1.Foods (Basel, Switzerland) · 2021Article
- Structure and Zeatin Binding of the Peach AllergenJournal of agricultural and food chemistry · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
A major proportion of allergic reactions to hazelnuts (Corylus avellana) are caused by immunologic cross-reactivity of IgE antibodies to pathogenesis-related class 10 (PR-10) proteins. Intriguingly, the four known isoforms of the hazelnut PR-10 allergen Cor a 1, denoted as Cor a 1.0401-Cor a 1.0404, share sequence identities exceeding 97% but possess different immunologic properties. In this work we describe the NMR solution structures of these proteins and provide an in-depth study of their biophysical properties. Despite sharing highly similar three-dimensional structures, the four isoforms exhibit remarkable differences regarding structural flexibility, hydrogen bonding and thermal stability. Our experimental data reveal an inverse relation between structural flexibility and IgE-binding in ELISA experiments, with the most flexible isoform having the lowest IgE-binding potential, while the isoform with the most rigid backbone scaffold displays the highest immunologic reactivity. These results point towards a significant entropic contribution to the process of antibody binding.
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