Structure, function and IgE epitopes of the peanut pan allergen Ara h 8
International Conference on Food Safety and Regulatory Measures
August 17-19, 2015 Birmingham, UK

Barry K Hurlburt

Southern Regional Research Center, USA

Posters-Accepted Abstracts: J Food Process Technol


The incidence of peanut allergy continues to rise in the US and Europe. Whereas exposure to the major allergens Ara h 1, 2, 3 and 6 can cause fatal anaphylaxis, exposure to the minor allergens usually does not. Ara h 8 is a minor allergen. Importantly, it is the minor food allergens that are thought to be responsible for Oral Allergy Syndrome (OAS) in which sensitization to airborne allergens causes a Type 2 allergic reaction to ingested foods. Furthermore, it is believed that similar protein structure rather than a similar linear sequence is the cause of OAS. Bet v 1 from birch pollen is a common sensitizing agent and OAS results when patients consume certain fruits, vegetables, tree nuts and peanuts. Here, we report the 3-dimensional structure of Ara h 8, a Bet v 1 homolog. The overall fold is very similar to that of Bet v 1, Api g 1 (celery), Glym 4 (soy) and Pruav 1 (cherry). Ara h 8 binds the isoflavones quercetin and apigeninas well as resveratrol avidly. Using micro-chip technology we have mapped the important linear epitopes for IgE binding.

Biography :

Email: Barry.Hurlburt@ARS.USDA.GOV