Hydrogen peroxide oxidation modifies the structural properties and allergenicity of the bee pollen allergen profilin

Bee pollen is a byproduct of pollination, which is a necessary process to produce foods. However, bee pollen can induce significant food-borne allergies. We previously identified a bee pollen-derived pan-allergen in the profilin family, Bra c p. Herein, we aimed to reduce Bra c p allergenicity via protein oxidation with hydrogen peroxide and explore the changes induced. Ion-mobility mass spectrometry revealed aggregation of the oxidized product; we also found irreversible sulfonation of the free sulfhydryl group of the Bra c p Cys98 residue to a more stable cysteine derivative. A significant proportion of the α-helices in Bra c p were transformed into β-sheets after oxidation, masking the antigenic epitopes. An immunoassay demonstrated that the IgE-binding affinity of Bra c p was decreased in vitro after oxidation. To our knowledge, this is the first report describing the application of protein oxidation to reduce the allergenicity of profilin family member in foods.