Abstract
In the last few years Ostrya carpinifolia pollen is considered as an important cause of respiratory allergy in Mediterranean areas. The concentration of the pollen was measured over a period of fifteen years from 1981 to 1996 in an area around Genoa; the results of this study have clearly indicated an increasing trend that correlate with persons sensitization. In this study we sought to define the immunochemical and biochemical properties of hop-hornbean pollen. Soluble proteins extracted from Ostrya carpinifolia pollen and from the taxonomically related species Corylus Avellana, were analyzed by polyacrylamide gel electrophoresis (SDS-PAGE), by horizontal isoelectrofocusing (IEF) and by two dimensions electrophoresis (2D-PAGE). Allergenic proteins were identified with sera of sensibilized patients and cross-reactivity was evaluated by immunoblotting techniques. The electrophoretic analysis showed a partial identity between the proteins from Ostrya and Corylus extracts. The immunoblotting assay, developed with human IgE from subjects allergic to hop-hornbeam pollen, displayed the major IgE reactivity for a component with a molecular weight of 17 kDa expressed in both Ostrya and Corylus extracts. This reactivity is consistent with the presence of Bet v 1 that is described as the major pollen allergen in the Betulaceae and Corylaceae families. Sera from subjects allergic to Ostrya were then preadsorbed with recombinant Bet v 1 immobilized in the Pharmacia CAP System; a significant reduction of the IgE binding activity was observed after the treatment. We therefore suggest that Bet v 1 could be one of the allergenic proteins present in the Ostrya pollen possibly being responsible for cross-reactivity with other members of taxonomically related families.
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