Structural highlights
Publication Abstract from PubMed
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.
Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.,Fuhrer S, Kamenik AS, Zeindl R, Nothegger B, Hofer F, Reider N, Liedl KR, Tollinger M Sci Rep. 2021 Feb 18;11(1):4173. doi: 10.1038/s41598-021-83705-z. PMID:33603065[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fuhrer S, Kamenik AS, Zeindl R, Nothegger B, Hofer F, Reider N, Liedl KR, Tollinger M. Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens. Sci Rep. 2021 Feb 18;11(1):4173. doi: 10.1038/s41598-021-83705-z. PMID:33603065 doi:http://dx.doi.org/10.1038/s41598-021-83705-z
