Unknown

Dataset Information

0

Structure and Zeatin Binding of the Peach Allergen Pru p 1.


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.

SUBMITTER: Eidelpes R 

PROVIDER: S-EPMC8323099 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure and Zeatin Binding of the Peach Allergen <i>Pru p 1</i>.

Eidelpes Reiner R   Hofer Florian F   Röck Manuel M   Führer Sebastian S   Kamenik Anna Sophia AS   Liedl Klaus R KR   Tollinger Martin M  

Journal of agricultural and food chemistry 20210714 29


Peach (<i>Prunus persica</i>) 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 <i>Pru p 1</i> (isoform Pru p 1.0101). This 17.5 kDa protein adopts the canonical Bet v  ...[more]

Similar Datasets

| S-EPMC6439177 | biostudies-literature
| S-EPMC7082028 | biostudies-literature
| S-EPMC8120414 | biostudies-literature
| S-EPMC6020533 | biostudies-literature
| S-EPMC8376049 | biostudies-literature
| S-EPMC8247360 | biostudies-literature
| S-EPMC8569022 | biostudies-literature
| S-EPMC9234939 | biostudies-literature
| S-EPMC5691307 | biostudies-literature
| S-EPMC5573991 | biostudies-literature