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Structure and Zeatin Binding of the Peach Allergen Pru p 1

[Image: see text] Peach (Prunus persica) is among the fruits most frequently reported to cause food allergies. Allergic reactions commonly result from previous sensitization to the birch pollen allergen Bet v 1, followed by immunological cross-reactivity of IgE antibodies to structurally related pro...

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Autores principales: Eidelpes, Reiner, Hofer, Florian, Röck, Manuel, Führer, Sebastian, Kamenik, Anna Sophia, Liedl, Klaus R., Tollinger, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8323099/
https://www.ncbi.nlm.nih.gov/pubmed/34260238
http://dx.doi.org/10.1021/acs.jafc.1c01876
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author Eidelpes, Reiner
Hofer, Florian
Röck, Manuel
Führer, Sebastian
Kamenik, Anna Sophia
Liedl, Klaus R.
Tollinger, Martin
author_facet Eidelpes, Reiner
Hofer, Florian
Röck, Manuel
Führer, Sebastian
Kamenik, Anna Sophia
Liedl, Klaus R.
Tollinger, Martin
author_sort Eidelpes, Reiner
collection PubMed
description [Image: see text] Peach (Prunus persica) is among the fruits most frequently reported to cause food allergies. Allergic reactions commonly result from previous sensitization to the birch pollen allergen Bet v 1, followed by immunological cross-reactivity of IgE antibodies to structurally related proteins in peach. In this study, we present the three-dimensional NMR solution structure of the cross-reactive peach allergen Pru p 1 (isoform Pru p 1.0101). This 17.5 kDa protein adopts the canonical Bet v 1 fold, composed of a seven-stranded β-sheet and three α-helices enclosing an internal cavity. In Pru p 1, the inner surface of the cavity contains an array of hydroxyl-bearing amino acids surrounded by a hydrophobic patch, constituting a docking site for amphiphilic molecules. NMR-guided docking of the cytokinin molecule zeatin to the internal cavity of Pru p 1 provides a structure-based rationale for the effect that zeatin binding has on the protein’s RNase activity.
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spelling pubmed-83230992021-08-02 Structure and Zeatin Binding of the Peach Allergen Pru p 1 Eidelpes, Reiner Hofer, Florian Röck, Manuel Führer, Sebastian Kamenik, Anna Sophia Liedl, Klaus R. Tollinger, Martin J Agric Food Chem [Image: see text] Peach (Prunus persica) is among the fruits most frequently reported to cause food allergies. Allergic reactions commonly result from previous sensitization to the birch pollen allergen Bet v 1, followed by immunological cross-reactivity of IgE antibodies to structurally related proteins in peach. In this study, we present the three-dimensional NMR solution structure of the cross-reactive peach allergen Pru p 1 (isoform Pru p 1.0101). This 17.5 kDa protein adopts the canonical Bet v 1 fold, composed of a seven-stranded β-sheet and three α-helices enclosing an internal cavity. In Pru p 1, the inner surface of the cavity contains an array of hydroxyl-bearing amino acids surrounded by a hydrophobic patch, constituting a docking site for amphiphilic molecules. NMR-guided docking of the cytokinin molecule zeatin to the internal cavity of Pru p 1 provides a structure-based rationale for the effect that zeatin binding has on the protein’s RNase activity. American Chemical Society 2021-07-14 2021-07-28 /pmc/articles/PMC8323099/ /pubmed/34260238 http://dx.doi.org/10.1021/acs.jafc.1c01876 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Eidelpes, Reiner
Hofer, Florian
Röck, Manuel
Führer, Sebastian
Kamenik, Anna Sophia
Liedl, Klaus R.
Tollinger, Martin
Structure and Zeatin Binding of the Peach Allergen Pru p 1
title Structure and Zeatin Binding of the Peach Allergen Pru p 1
title_full Structure and Zeatin Binding of the Peach Allergen Pru p 1
title_fullStr Structure and Zeatin Binding of the Peach Allergen Pru p 1
title_full_unstemmed Structure and Zeatin Binding of the Peach Allergen Pru p 1
title_short Structure and Zeatin Binding of the Peach Allergen Pru p 1
title_sort structure and zeatin binding of the peach allergen pru p 1
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8323099/
https://www.ncbi.nlm.nih.gov/pubmed/34260238
http://dx.doi.org/10.1021/acs.jafc.1c01876
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