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Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family

PURPOSE OF REVIEW: Pathogenesis-related class 10 (PR-10) proteins are highly conserved plant proteins, which are induced in response to abiotic and biotic stress factors. To date, no unique biological function could be assigned to them. Rather a more general role of PR-10 in plant development and de...

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Autores principales: Aglas, Lorenz, Soh, Wai Tuck, Kraiem, Amin, Wenger, Mario, Brandstetter, Hans, Ferreira, Fatima
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7237532/
https://www.ncbi.nlm.nih.gov/pubmed/32430735
http://dx.doi.org/10.1007/s11882-020-00918-4
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author Aglas, Lorenz
Soh, Wai Tuck
Kraiem, Amin
Wenger, Mario
Brandstetter, Hans
Ferreira, Fatima
author_facet Aglas, Lorenz
Soh, Wai Tuck
Kraiem, Amin
Wenger, Mario
Brandstetter, Hans
Ferreira, Fatima
author_sort Aglas, Lorenz
collection PubMed
description PURPOSE OF REVIEW: Pathogenesis-related class 10 (PR-10) proteins are highly conserved plant proteins, which are induced in response to abiotic and biotic stress factors. To date, no unique biological function could be assigned to them. Rather a more general role of PR-10 in plant development and defense mechanisms has been proposed. In addition, some PR-10 proteins act as allergens by triggering allergic symptoms in sensitized individuals. Regardless of the diversity of reported activities, all PR-10 proteins share a common fold characterized by a solvent-accessible hydrophobic cavity, which serves as a binding site for a myriad of small-molecule ligands, mostly phytohormones and flavonoids. RECENT FINDINGS: Most of available data relate to the ligand binding activity of allergenic PR-10, particularly for those belonging to Bet v 1 family of allergens. Bet v 1 and its homologues were shown to bind flavonoids with high affinity, but the specificity appears to differ between homologues from different species. The flavonoid Q3O-(Glc)-Gal was shown to specifically bind to hazelnut Cor a 1 but not to Bet v 1. Similarly, Q3OS bound only to the major isoform Bet v 1.0101 and not to other closely related isoforms. In contrast, Bet v 1 and hazelnut Cor a 1 showed very similar binding behavior towards other flavonoids such as quercetin, genistein, apigenin, daidzein, and resveratrol. SUMMARY: Recent research findings highlighted the importance of more precise knowledge of ligand binding for understanding the functional diversification of PR-10 proteins.
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spelling pubmed-72375322020-05-27 Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family Aglas, Lorenz Soh, Wai Tuck Kraiem, Amin Wenger, Mario Brandstetter, Hans Ferreira, Fatima Curr Allergy Asthma Rep Allergens (RK Bush and S Vieths, Section Editors) PURPOSE OF REVIEW: Pathogenesis-related class 10 (PR-10) proteins are highly conserved plant proteins, which are induced in response to abiotic and biotic stress factors. To date, no unique biological function could be assigned to them. Rather a more general role of PR-10 in plant development and defense mechanisms has been proposed. In addition, some PR-10 proteins act as allergens by triggering allergic symptoms in sensitized individuals. Regardless of the diversity of reported activities, all PR-10 proteins share a common fold characterized by a solvent-accessible hydrophobic cavity, which serves as a binding site for a myriad of small-molecule ligands, mostly phytohormones and flavonoids. RECENT FINDINGS: Most of available data relate to the ligand binding activity of allergenic PR-10, particularly for those belonging to Bet v 1 family of allergens. Bet v 1 and its homologues were shown to bind flavonoids with high affinity, but the specificity appears to differ between homologues from different species. The flavonoid Q3O-(Glc)-Gal was shown to specifically bind to hazelnut Cor a 1 but not to Bet v 1. Similarly, Q3OS bound only to the major isoform Bet v 1.0101 and not to other closely related isoforms. In contrast, Bet v 1 and hazelnut Cor a 1 showed very similar binding behavior towards other flavonoids such as quercetin, genistein, apigenin, daidzein, and resveratrol. SUMMARY: Recent research findings highlighted the importance of more precise knowledge of ligand binding for understanding the functional diversification of PR-10 proteins. Springer US 2020-05-19 2020 /pmc/articles/PMC7237532/ /pubmed/32430735 http://dx.doi.org/10.1007/s11882-020-00918-4 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Allergens (RK Bush and S Vieths, Section Editors)
Aglas, Lorenz
Soh, Wai Tuck
Kraiem, Amin
Wenger, Mario
Brandstetter, Hans
Ferreira, Fatima
Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
title Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
title_full Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
title_fullStr Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
title_full_unstemmed Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
title_short Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
title_sort ligand binding of pr-10 proteins with a particular focus on the bet v 1 allergen family
topic Allergens (RK Bush and S Vieths, Section Editors)
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7237532/
https://www.ncbi.nlm.nih.gov/pubmed/32430735
http://dx.doi.org/10.1007/s11882-020-00918-4
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