Barry K Hurlburt
United States Department of Agriculture, USA
Title: Ligand binding preferences of pathogenesis-related class 10 (pr-10) allergens
Biography
Biography: Barry K Hurlburt
Abstract
Rationale: Many PR-10 proteins are allergens when inhaled or ingested. One proposed function of these proteins is delivering bio-active compounds to wounds and/or the developing plant. We examined ligand binding to seven known PR-10 allergens. Ligand binding could well affect IgE binding. Methods: We generated pure, recombinant Ara h 8.01, Ara h 8.02, Cor a 1.02, Cor a 1.04, Que a 1.02, Que a 1.03 and Bet v 1.01 from peanut, hazelnut, white oak and birch respectively. Twenty three putative ligands were tested for binding using a fluorescence assay. Results: All of the proteins bound apigenin, daidzein, genistein, quercetin and resveratrol. Que a 1.03 bound the widest array of ligands including several fatty acids. Preliminary structural studies show changes in protein structure with ligand binding. Conclusions: Our results support the theory that these PR-10 allergens’ function in vivo is as a delivery vehicle for bio-active compounds. Now that we have identified biologically-relevant ligands we will test the possibility that binding them to PR-10 proteins may influence allergenic potential.
