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Review
. 2020 May 19;20(7):25.
doi: 10.1007/s11882-020-00918-4.

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

Lorenz Aglas  1 , Wai Tuck Soh  1   2 , Amin Kraiem  1 , Mario Wenger  1 , Hans Brandstetter  1 , Fatima Ferreira  3
Affiliations
Review

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

Lorenz Aglas et al. Curr Allergy Asthma Rep. .

Abstract

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. Recent research findings highlighted the importance of more precise knowledge of ligand binding for understanding the functional diversification of PR-10 proteins.

Keywords: Allergens; Bet v 1; Cytokinin; Flavonoid; Ligand; PR-10.

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Conflict of interest statement

Dr. Ferreira reports personal fees from HAL Allergy, Swiss Institute of Allergy and Asthma Research, and AllergenOnline, outside the submitted work. The other authors declare no conflicts of interest relevant to this manuscript.

Figures

Fig. 1
Fig. 1
Overview on described functions associated with PR-10 ligand binding; PR-10, pathogenesis-related proteins class 10; IPR, intracellular pathogenesis-related proteins/classic PR-10 proteins; CSBP, cytokinin-specific binding proteins; MLP, major latex proteins; other PR-10-like, not yet classified proteins possessing a PR-10-like fold
See this image and copyright information in PMC

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