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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #298323
Title: Structure and function of the peanut panallergen Ara h 8

Author
item Hurlburt, Barry
item OFFERMANN, LESA - University Of South Carolina
item McBride, Jane
item MAJOREK, KAROLINA - University Of Virginia
item Maleki, Soheila
item CHRUSZCZ, MAKSYMILIAN - University Of South Carolina

Submitted to: Journal of Biological Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/18/2013
Publication Date: 2/11/2014
Citation: Hurlburt, B.K., Offermann, L.R., Mcbride, J.K., Majorek, K.A., Maleki, S.J., Chruszcz, M. 2014. Structure and function of the peanut panallergen Ara h 8. Journal of Biological Chemistry. 288:36890-36901.

Interpretive Summary: The incidence of peanut allergy continues to rise in the U.S. and Europe; whereas, exposure to the major allergen proteins 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 an allergic reaction to ingested foods. In this work we determined the 3-dimensional structure of Ara h 8. We also found that Ara h 8 can bind hydrophobic molecules.

Technical Abstract: 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 p\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), Gly m 4 (soy), and Pru av 1 (cherry). Ara h 8 binds the isoflavones quercetin and apigenin, as well as resveratrol avidly.