Abstract
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.
Highlights
Consumption of peach (Prunus persica) can elicit allergic reactions in atopic patients.[1,2] Peach-allergic patients avoid eating these fruits, abstaining themselves from a valuable food source of high nutritive and health value
In Central and Northern Europe, peach allergy is strongly associated with birch pollinosis, resulting from initial sensitization to the major birch (Betula verrucosa) pollen allergen Bet v 1, followed by immunologic cross-reaction of IgE antibodies against Bet v 1 with structurally related proteins in peach.[3]
The allergen that triggers birch-pollen-related food allergies (BPRFA) in peach is the 17.5 kDa protein Pru p 1.5 Pru p 1, like Bet v 1, belongs to the class 10 of pathogenesis-related (PR) proteins that are activated in plants in response to abiotic and biotic stress.[6]
Summary
Consumption of peach (Prunus persica) can elicit allergic reactions in atopic patients.[1,2] Peach-allergic patients avoid eating these fruits, abstaining themselves from a valuable food source of high nutritive and health value.
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