Volume 4 Supplement 2

5th International Symposium on Molecular Allergology (ISMA 2013)

Open Access

Structural changes induced by heating affect ovalbumin-antigen processing and reduce allergic response in mouse model of food allergy

  • Jaroslav Goliáš1,
  • Martin Schwarzer2,
  • Hana Kozáková2,
  • Dagmar Šrùtková2 and
  • Ludmila Tuèková1
Clinical and Translational Allergy20144(Suppl 2):P25

https://doi.org/10.1186/2045-7022-4-S2-P25

Published: 17 March 2014

Background

Food allergy is a serious health concern affecting about 8% of young children and about 3% of adults. The egg protein ovalbumin belongs among six frequent food allergens. Our goal was to develop the mouse model of ovalbumin food allergy and investigate how thermal processing affects its ability to induce allergic responses.

Methods

Effect of thermal processing (70°C and 95°C) on an ovalbumin secondary structure was characterized by circular dichroism and by kinetics of pepsin digestion with subsequent HPLC analysis. BALB/c mice were sensitized intraperitoneally and challenged intragastrically with native form or thermal processed ovalbumin (70°C). Clinical symptoms (allergic diarrhea, weight and temperature) were observed during the mice challenging. Levels of allergen-specific serum antibodies were determined by ELISA (IgA, IgG1 and IgG2a) by beta-hexosaminidase release test (IgE). Cytokine production (IL-4, IL-5, IL-6, IL-10, IL-13, IL-17, IFN-gamma) and mast cell protease-1 activity were assessed by ELISA. The activities of brush-border hydrolases were determined in the jejunum of treated mice.

Results

Heating of ovalbumin caused slight irreversible changes in secondary structure and significantly decreased clinical symptoms (allergic diarrhea). The thermal processing also decreased immune allergic response on the level of IgE, IL-4, IL-5, IL-13. Furthermore, thermal-processed ovalbumin induced lower activities of serum mast cell protease-1 and enterocyte brush border membrane alkaline phosphatase as compared to native ovalbumin. On the other hand, thermal-processed ovalbumin stimulated higher IgG2a antibodies in sera and IFN-gamma secretion by splenocytes.

Conclusion

In our mice model of food allergy, we show that even a slight change in the secondary structure of ovalbumin after thermal processing reduces its allergenicity and induces shift towards Th1 immune responses. At present, we utilize this model for studying of food allergy in germ-free mice.

Authors’ Affiliations

(1)
Department of Immunology and Gnotobiology, Institute of Microbiology, The Academy of Sciences of the Czech Republic
(2)
Department of Immunology and Gnotobiology, Institute of Microbiology, The Academy of Sciences of the Czech Republic

Copyright

© Goliáš et al; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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