- Poster presentation
- Open Access
Proteomic and immunoassay characterization of a new food allergen from hazelnut (corylus avellana)
© Picariello et al; licensee BioMed Central Ltd. 2013
- Published: 25 July 2013
- Food Allergy
- Crude Protein Extract
- Oral Food Challenge
- Oral Allergy Syndrome
- Corylus Avellana
Hazelnut (Corylus avellana) is a common cause of lifetime lasting IgE-mediated food allergy. Symptoms range from mild oral allergy syndrome to severe life-threatening anaphylaxis. We aimed to identify allergenic determinants in children living in the Campania region (Italy) with hazelnut allergy.
Otherwise healthy children with oral food challenge confirmed hazelnut allergy were prospectively evaluated. Crude protein extracts were obtained from 5 hazelnut varieties, including autochthon, Northern Italy and Oregon (USA) cultivars, with phosphate saline buffer, pH 7.2. The immunoreactive protein components were identified by SDS-PAGE electrophoresis and Western immunoblotting, using patients sera as source of specific IgE. The IgE-binding protein bands were characterized by advanced proteomic strategies and tandem mass spectrometry (MS)-based de novo peptide sequencing.
Four subjects were evaluated (2 male, 50%; mean age 39 m). Symptoms were: urticaria (2), angioedema (3), anaphylaxis (2). No significant differences were observed considering the main demographic and clinical characteristics at diagnosis. All children’s sera were immunoreactive to a protein, not previously annotated in database, occurring in hazelnut regardless the variety. The allergen was isolated by combined chromatographic strategies. Only one patient exhibited an additional reactivity to the vicilin-like 7S 48 kDa glycoprotein (Cor a 11). The MS-based characterization provided evidence of a high homology degree between the IgE-binding protein subunit and 11S globulin-like storage proteins expressed in other seeds. The new allergen shares structural traits with the hazelnut 11S globulin-like proteins (Cor a 9) such as the disulfide linkage of two subunits, an acidic (~35 kDa) and an alkaline (~21 kDa) one. Interestingly, only the alkaline subunit exhibits antigenic properties.
A previously unrecognized hazelnut allergen was identified. Except for a faint IgE reactivity of Cor a 11 recorded in a single case, the new allergen was the unique IgE-binding protein in our patients. Future study are warranted to better define possible prognostic and immunotherapeutic implications.
This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.