TY - JOUR
T1 - Peamaclein - A new peach allergenic protein
T2 - Similarities, differences and misleading features compared to Pru p 3
AU - Tuppo, L.
AU - Alessandri, C.
AU - Pomponi, D.
AU - Picone, D.
AU - Tamburrini, M.
AU - Ferrara, R.
AU - Petriccione, M.
AU - Mangone, I.
AU - Palazzo, P.
AU - Liso, M.
AU - Giangrieco, I.
AU - Crescenzo, R.
AU - Bernardi, M. L.
AU - Zennaro, D.
AU - Helmer-Citterich, M.
AU - Mari, A.
AU - Ciardiello, M. A.
PY - 2013/1
Y1 - 2013/1
N2 - Background: 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. Objective: To identify and characterize a new peach allergen causing a clinical picture similar to that of Pru p 3. Methods: 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. Results: 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 in vivo 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. Conclusions and Clinical Relevance: 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.
AB - Background: 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. Objective: To identify and characterize a new peach allergen causing a clinical picture similar to that of Pru p 3. Methods: 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. Results: 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 in vivo 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. Conclusions and Clinical Relevance: 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.
KW - Allergen
KW - Cysteine-rich protein
KW - Direct protein sequencing
KW - Inhibition
KW - Microarray
KW - New allergenic protein family
KW - Peach
KW - Severe food allergy
KW - Stability
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U2 - 10.1111/cea.12028
DO - 10.1111/cea.12028
M3 - Article
C2 - 23278887
AN - SCOPUS:84871693164
VL - 43
SP - 128
EP - 140
JO - Clinical and Experimental Allergy
JF - Clinical and Experimental Allergy
SN - 0954-7894
IS - 1
ER -