Unknown

Dataset Information

0

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


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.

SUBMITTER: Fuhrer S 

PROVIDER: S-EPMC7892832 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Führer Sebastian S   Kamenik Anna S AS   Zeindl Ricarda R   Nothegger Bettina B   Hofer Florian F   Reider Norbert N   Liedl Klaus R KR   Tollinger Martin M  

Scientific reports 20210218 1


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 bio  ...[more]

Similar Datasets

| S-EPMC6381869 | biostudies-literature
| S-EPMC7902920 | biostudies-literature
| S-EPMC4616228 | biostudies-literature
| S-EPMC9330593 | biostudies-literature
| S-EPMC3203311 | biostudies-literature
| S-EPMC7493343 | biostudies-literature
| S-EPMC5617217 | biostudies-other
| S-EPMC7031643 | biostudies-literature
| S-EPMC6264518 | biostudies-literature
| S-EPMC2628846 | biostudies-literature