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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2021
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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. |
format | Online Article Text |
id | pubmed-8323099 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
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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