Peamaclein – A new peach allergenic protein: similarities, differences and misleading features compared to Pru p 3. Issue 1 (24th December 2012)

• Record Type: Journal Article
• Authors: Tuppo, L.; Alessandri, C.; Pomponi, D.; Picone, D.; Tamburrini, M.; Ferrara, R.; Petriccione, M.; Mangone, I.; Palazzo, P.; Liso, M.; Giangrieco, I.; Crescenzo, R.; Bernardi, M. L.; Zennaro, D.; Helmer‐Citterich, M.; Mari, A.; Ciardiello, M. A.
• Is Part Of: Clinical & experimental allergy. Volume 43:Issue 1(2013:Jan.)
• Page Start: 128
• Page End: 140
• Publication Date: 2012-12-24
• Subjects: Allergy -- Periodicals; Immunology -- Periodicals; 616.97
• DOI: 10.1111/cea.12028
• Languages: English
• ISSNs: 0954-7894

Abstract

<abstract abstract-type="main" id="cea12000-abs-0001"> <title>Summary</title> <sec id="cea12028-sec-0001" sec-type="section"> <title>Background</title> <p>Among the peach‐derived allergens which are already known, the lipid transfer protein (Pru p 3) seems to be the one to exert severe allergic reactions.</p> </sec> <sec id="cea12028-sec-0002" sec-type="section"> <title>Objective</title> <p>To identify and characterize a new peach allergen causing a clinical picture similar to that of Pru p 3.</p> </sec> <sec id="cea12028-sec-0003" sec-type="section"> <title>Methods</title> <p>Patients were selected on the basis of their severe clinical reactivity and negative results to a panel of peach allergens available on the ISAC103 microarray. Several in‐house and commercial preparations were compared. Several methods were used to characterize the newly identified molecule. Specific IgE and inhibition assays were performed using the Allergen micro‐Beads Array (ABA) assay.</p> </sec> <sec id="cea12028-sec-0004" sec-type="section"> <title>Results</title> <p>Negative ISAC results to Pru p 3 were confirmed by additional testing in contrast with the positive results obtained by commercial Pru p 3‐enriched peach peel extracts. The analyses of one of these preparations led to the identification of Peamaclein, a new allergenic protein. It is a small, basic, cysteine‐rich, heat‐stable, digestion‐resistant protein, homologous to a potato antimicrobial peptide. Peamaclein was able to trigger positive skin test reactions and to bind IgE in the ABA assay. It displays an electrophoretic mobility and chromatographic behaviour similar to that of Pru p 3; therefore, it can be hidden in Pru p 3 preparations. In fact, Pru p 3‐enriched peach peel extracts were found to contain both Pru p 3 and Peamaclein by means of comparative <italic>in vivo</italic> testing, and by biochemical and immunochemical assays. Commercially available anti‐Pru p 3 polyclonal antibodies were found to have a double specificity for the two molecules.</p> </sec> <sec id="cea12028-sec-0005" sec-type="section"> <title>Conclusions and Clinical Relevance</title> <p>A new allergen from peach belonging to a new family of allergenic proteins has been identified and characterized. This knowledge on Peamaclein will improve our understanding on the clinical aspects of the peach allergy and the quality of diagnostic reagents.</p> </sec> </abstract>