Details

Autor(en) / Beteiligte

• Pastorello, Elide A.
• Vieths, Stefan
• Pravettoni, Valerio
• Farioli, Laura
• Trambaioli, Chiara
• Fortunato, Donatella
• Lüttkopf, Dirk
• Calamari, Marianna
• Ansaloni, Raffaella
• Scibilia, Joseph
• Ballmer-Weber, Barbara K.
• Poulsen, Lars K.
• Wütrich, Brunello
• Hansen, Kirsten Skamstrup
• Robino, Anna Maria
• Ortolani, Claudio
• Conti, Amedeo

Titel

Identification of hazelnut major allergens in sensitive patients with positive double-blind, placebo-controlled food challenge results

Ist Teil von

• Journal of allergy and clinical immunology, 2002-03, Vol.109 (3), p.563-570

Ort / Verlag

New York, NY: Mosby, Inc

Erscheinungsjahr

2002

Quelle

Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)

Beschreibungen/Notizen

• Background: The hazelnut major allergens identified to date are an 18-kd protein homologous to Bet v 1 and a 14-kd allergen homologous to Bet v 2. No studies have reported hazelnut allergens recognized in patients with positive double-blind, placebo-controlled food challenge (DBPCFC) results or in patients allergic to hazelnut but not to birch. Objective: We characterized the hazelnut allergens by studying the IgE reactivity of 65 patients with positive DBPCFC results and 7 patients with severe anaphylaxis to hazelnut. Methods: Hazelnut allergens were identified by means of SDS-PAGE and IgE immunoblotting. Further characterization was done with amino acid sequencing, evaluation of the IgE-binding properties of raw and roasted hazelnut with enzyme allergosorbent test inhibition, assessment of cross-reactivity with different allergens by means of immunoblotting inhibition, and purification by means of HPLC. Results: All the sera from the patients with positive DBPCFC results recognized an 18- and a 47-kd allergen; other major allergens were at molecular weights of 32 and 35 kd. Binding to the 18-kd band was inhibited by birch extract, indicating its homology with the birch major allergen, and abolished in roasted hazelnut. The 47-kd allergen is a sucrose-binding protein, the 35-kd allergen is a legumin, and the 32-kd allergen is a 2S albumin. Patients with severe anaphylactic reactions to hazelnut showed specific IgE reactivity to a 9-kd allergen, totally inhibited by purified peach lipid-transfer protein (LTP), which was heat stable and, when purified, corresponded to an LTP. Conclusions: The major allergen of hazelnut is an 18-kd protein homologous to Bet v 1, and the 9-kd allergen is presumably an LTP. Other major allergens have molecular weights of 47, 32, and 35 kd. (J Allergy Clin Immunol 2002;109:563-70.)