Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens

• DOI: 10.1038/s41598-021-83705-z
• Publication Date: 2021-02-20T09:14:59Z
• Authors: Sebastian Führer; Anna S. Kamenik; Ricarda Zeindl; Bettina Nothegger; Florian Hofer; Norbert Reider; Klaus R. Liedl; Martin Tollinger
• Keywords: 0301 basic medicine; Science; Q; R; Allergens; Antigens, Plant; Cross Reactions; Immunoglobulin E; Article; 03 medical and health sciences; Corylus; Hypersensitivity; Medicine; Protein Isoforms; Amino Acid Sequence; Plant Proteins

A major proportion of allergic reactions to hazelnuts (Corylus avellana) are caused by immunologic cross-reactivity IgE antibodies pathogenesis-related class 10 (PR-10) proteins. Intriguingly, the four known isoforms hazelnut PR-10 allergen Cor a 1, denoted as 1.0401-Cor 1.0404, share sequence identities exceeding 97% but possess different properties. In this work we describe NMR solution structures these proteins and provide an in-depth study their biophysical Despite sharing highly similar three-dimensional structures, exhibit remarkable differences regarding structural flexibility, hydrogen bonding thermal stability. Our experimental data reveal inverse relation between flexibility IgE-binding in ELISA experiments, with most flexible isoform having lowest potential, while rigid backbone scaffold displays highest reactivity. These results point towards significant entropic contribution process antibody binding.