| Literature DB >> 24996302 |
Jana Ognjenović1, Marija Stojadinović2, Miloš Milčić2, Danijela Apostolović2, Jelena Vesić2, Ivan Stambolić2, Marina Atanasković-Marković3, Miljan Simonović4, Tanja Cirkovic Velickovic2.
Abstract
Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells.Entities:
Keywords: Epigallo-catechin 3-gallate; Fluorophore quenching; Food allergy; IgE binding; Molecular docking; Monocytes; Ovalbumin
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Year: 2014 PMID: 24996302 DOI: 10.1016/j.foodchem.2014.05.005
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514