Title
Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy
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.
van Ree, R.
Vieths, S.
TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO
Publication year
2004
Abstract
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.
Subject
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
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DOI
https://doi.org/10.1016/j.jaci.2004.09.014
TNO identifier
238247
ISSN
0091-6749
Source
Journal of Allergy and Clinical Immunology, 114 (6), 1410-1417
Document type
article