Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white
Authorized Users Only
2014
Authors
Ognjenović, JanaStojadinović, Marija M.
Milčić, Miloš K.

Apostolović, Danijela

Mihailović-Vesić, Jelena

Stambolić, Ivan
Atanasković-Marković, Marina
Simonovic, Miljan

Ćirković-Veličković, Tanja

Article (Published version)

Metadata
Show full item recordAbstract
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. (C) 2014 Elsevier Ltd. All rig...hts reserved.
Keywords:
Epigallo-catechin 3-gallate / Food allergy / IgE binding / Fluorophore quenching / Molecular docking / Monocytes / OvalbuminSource:
Food Chemistry, 2014, 164, 36-43Publisher:
- Elsevier Sci Ltd, Oxford
Projects:
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
DOI: 10.1016/j.foodchem.2014.05.005
ISSN: 0308-8146
PubMed: 24996302