6z98

Publication Abstract from PubMed

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 beta-sheet and three alpha-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.

Structure and Zeatin Binding of the Peach Allergen Pru p 1.,Eidelpes R, Hofer F, Rock M, Fuhrer S, Kamenik AS, Liedl KR, Tollinger M J Agric Food Chem. 2021 Jul 28;69(29):8120-8129. doi: 10.1021/acs.jafc.1c01876., Epub 2021 Jul 14. PMID:34260238^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.