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J Agric Food Chem. 2008 Mar 26;56(6):2223-30. doi: 10.1021/jf072907n. Epub 2008 Feb 26.

Determination of pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated peanut allergen Ara h 1.

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Laboratory of Food Chemistry, Wageningen University, P.O. Box 8129, 6700 EV Wageningen, The Netherlands.


This study was aimed at the determination of the pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated Ara h 1, a major allergen from peanuts. Both the oligomeric structure and the trimeric structure of the allergen were investigated. Under the in vitro conditions applied, oligomeric Ara h 1, either unheated or preheated, was hydrolyzed by pepsin at a lower rate than trimeric Ara h 1. Peptides with relatively high molecular masses were shown to be able to bind IgE, whereas peptides with lower molecular masses (<2 kDa) did not. In these latter fractions, fragments of 15 previously published epitopes of mature Ara h 1 were identified. As a result, these epitopes are not likely responsible for the induction of systemic food allergic reactions to peanuts. Using sequential chymotrypsin digestion, the pepsin-resistant IgE-binding peptides were deduced to contain the previously identified intact epitopes EDWRRPSHQQ (amino acids 50-59) and PRKIRPEG (amino acids 60-67). The presence of four additional earlier published intact epitopes (covering amino acids 6-13, 14-21, 24-31, and 40-47) on the pepsin-resistant peptides could be neither deduced nor ruled out. The two deduced and four possible pepsin-resistant epitopes are all situated in the N-terminal part of Ara h 1, which does not show homology with other vicilin proteins. Consequently, this unique N-terminal part of Ara h 1 is proposed to be responsible for the allergen's ability to induce systemic allergic reactions.

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