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- W3131170082 abstract "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." @default.
- W3131170082 created "2021-03-01" @default.
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- W3131170082 date "2021-02-18" @default.
- W3131170082 modified "2023-10-14" @default.
- W3131170082 title "Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens" @default.
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- W3131170082 doi "https://doi.org/10.1038/s41598-021-83705-z" @default.
- W3131170082 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7892832" @default.
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- W3131170082 hasPublicationYear "2021" @default.
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