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Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy

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Author: Mittag, D. · Akkerdaas, J. · Ballmer-Weber, B.K. · Vogel, L. · Wensing, M. · Becker, W.M. · Koppelman, S.J. · Knulst, A.C. · Helbling, A. · Hefle, S.L. · Ree, R. van · Vieths, S.
Institution: TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO
Source:Journal of Allergy and Clinical Immunology, 6, 114, 1410-1417
Identifier: 238247
doi: doi:10.1016/j.jaci.2004.09.014
Keywords: Nutrition · Food technology · Ara h 8 · Birch pollen-related food allergy · Diagnosis · Double-blind · Gly m 4 · Legumes · Oral allergy syndrome · Peanut allergy · Placebo-controlled food challenge · Recombinant allergen · Allergen · Ara h 8 allergen · Bet v 1 allergen · Histamine · Unclassified drug · Adult · Amino acid sequence · Antigen antibody reaction · Antigen specificity · Basophil · Birch · Blood analysis · Clinical article · Controlled study · Cross linking · Cross reaction · Digestion · Female · Histamine release · Human · Immunoblotting · Male · Molecular cloning · Mouth cavity · Peanut allergy · Pollen allergy · Priority journal · Provocation test · Adolescent · Adult · Allergens · Amino Acid Sequence · Basophils · Betula · Cross Reactions · Double-Blind Method · Female · Histamine Release · Humans · Immunoglobulin E · Male · Molecular Sequence Data · Peanut Hypersensitivity · Pepsin A · Pollen · Recombinant Proteins


We recently described patients with soybean allergy mainly mediated by cross-reactivity to birch pollen allergens. A majority of those patients were reported to have peanut allergy. We sought to study the occurrence of peanut allergy in patients allergic to birch pollen and characterized the Bet v 1-homologous peanut allergen Ara h 8. Recombinant Ara h 8 was cloned with degenerated primers and expressed in Escherichia coli. Nine Swiss and 11 Dutch patients with peanut and birch pollen allergy and a positive double-blind, placebo-controlled food challenge result to peanut were investigated for IgE reactivity to birch pollen and purified peanut allergens and cross-reactivity between birch and peanut. Ara h 8 stability against digestion and roasting was assessed by means of RAST inhibition. The IgE cross-linking potency of Ara h 8 was tested on the basis of basophil histamine release. During double-blind, placebo-controlled food challenge, all patients experienced symptoms in the oral cavity, progressing to more severe symptoms in 40% of patients. CAP-FEIA detected recombinant (r) Ara h 8-specific IgE in 85%. IgE binding to Ara h 8 was inhibited by Bet v 1 in peanut extract immunoblotting and in RAST inhibition. In EAST inhibition recombinant rAra h 8 inhibited IgE binding to peanut in 4 of 7 tested patient sera. Antipeanut response was dominated by Ara h 8 in 12 of 17 tested patients. Furthermore, our results demonstrate a low stability of Ara h 8 to roasting and no stability to gastric digestion. Basophil histamine release with rAra h 8 was more than 20% in 5 of 7 tested sera. Peanut allergy might be mediated in a subgroup of our patients by means of cross-reaction of Bet v 1 with the homologous peanut allergen Ara h 8.