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...

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Autores principales:	Sebastian Führer, Anna S. Kamenik, Ricarda Zeindl, Bettina Nothegger, Florian Hofer, Norbert Reider, Klaus R. Liedl, Martin Tollinger
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/78310ff5a82443228d4ad45b082dd9ab
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spelling	oai:doaj.org-article:78310ff5a82443228d4ad45b082dd9ab2021-12-02T12:11:28ZInverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens10.1038/s41598-021-83705-z2045-2322https://doaj.org/article/78310ff5a82443228d4ad45b082dd9ab2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83705-zhttps://doaj.org/toc/2045-2322Abstract 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.Sebastian FührerAnna S. KamenikRicarda ZeindlBettina NotheggerFlorian HoferNorbert ReiderKlaus R. LiedlMartin TollingerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sebastian Führer Anna S. Kamenik Ricarda Zeindl Bettina Nothegger Florian Hofer Norbert Reider Klaus R. Liedl Martin Tollinger Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens
description	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.
format	article
author	Sebastian Führer Anna S. Kamenik Ricarda Zeindl Bettina Nothegger Florian Hofer Norbert Reider Klaus R. Liedl Martin Tollinger
author_facet	Sebastian Führer Anna S. Kamenik Ricarda Zeindl Bettina Nothegger Florian Hofer Norbert Reider Klaus R. Liedl Martin Tollinger
author_sort	Sebastian Führer
title	Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens
title_short	Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens
title_full	Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens
title_fullStr	Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens
title_full_unstemmed	Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens
title_sort	inverse relation between structural flexibility and ige reactivity of cor a 1 hazelnut allergens
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/78310ff5a82443228d4ad45b082dd9ab
work_keys_str_mv	AT sebastianfuhrer inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT annaskamenik inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT ricardazeindl inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT bettinanothegger inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT florianhofer inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT norbertreider inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT klausrliedl inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens AT martintollinger inverserelationbetweenstructuralflexibilityandigereactivityofcora1hazelnutallergens
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Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens

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