TY  - JOUR
AU  - Ognjenović, Jana
AU  - Stojadinović, Marija M.
AU  - Milčić, Miloš K.
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Stambolić, Ivan
AU  - Atanasković-Marković, Marina
AU  - Simonovic, Miljan
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1820
AB  - 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 rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white
VL  - 164
SP  - 36
EP  - 43
DO  - 10.1016/j.foodchem.2014.05.005
ER  - 

@article{
author = "Ognjenović, Jana and Stojadinović, Marija M. and Milčić, Miloš K. and Apostolović, Danijela and Mihailović-Vesić, Jelena and Stambolić, Ivan and Atanasković-Marković, Marina and Simonovic, Miljan and Ćirković-Veličković, Tanja",
year = "2014",
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. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white",
volume = "164",
pages = "36-43",
doi = "10.1016/j.foodchem.2014.05.005"
}

Ognjenović, J., Stojadinović, M. M., Milčić, M. K., Apostolović, D., Mihailović-Vesić, J., Stambolić, I., Atanasković-Marković, M., Simonovic, M.,& Ćirković-Veličković, T.. (2014). Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. in Food Chemistry
Elsevier Sci Ltd, Oxford., 164, 36-43.
https://doi.org/10.1016/j.foodchem.2014.05.005

Ognjenović J, Stojadinović MM, Milčić MK, Apostolović D, Mihailović-Vesić J, Stambolić I, Atanasković-Marković M, Simonovic M, Ćirković-Veličković T. Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. in Food Chemistry. 2014;164:36-43.
doi:10.1016/j.foodchem.2014.05.005 .

Ognjenović, Jana, Stojadinović, Marija M., Milčić, Miloš K., Apostolović, Danijela, Mihailović-Vesić, Jelena, Stambolić, Ivan, Atanasković-Marković, Marina, Simonovic, Miljan, Ćirković-Veličković, Tanja, "Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white" in Food Chemistry, 164 (2014):36-43,
https://doi.org/10.1016/j.foodchem.2014.05.005 . .