SummaryType I allergy to pollen of the European chestnut (Castanea sativa) represents a major cause of pollinosis in (sub) Mediterranean areas. Using sera from 14 patients with established allergy to pollen of the European chestnut, 13/14 sera (92) showed IgE‐binding to a 22 kD protein, 2/14(14) displayed additional binding to a 14 kD protein and 1/14 (7) bound only to the 14 kD protein of European chestnut pollen extract. Two monoclonal mouse antibodies, BIP 1 and BIP 4, directed against different epitopes ofBet vI (the major birch pollen allergen), and a rabbit antibody to recombinant birch profilin (rBet vII) were used to characterize the proteins of the European chestnut pollen. The recombinant birch pollen allergens, rBet vI and rBet vII (profilin) were employed to show common allergenic structures on proteins from both birch and European chestnut pollen by IgE‐inhibition experiments. Despite the fact that the 22 kD protein displayed a higher molecular weight in comparison to the 17 kD major birch pollen allergen,Bet vI, we could demonstrate reactivity of both monoclonal antibodies, BIP 1 and BIP 4, with this protein. A complete inhibiton of IgE‐binding to this 22 kD protein was shown by pre‐incubating sera with purified recombinantSetr I. In addition, the 14kD protein could be identified by IgE‐inhibition studies with recombinantBet vII and by using a rabbit anti‐profilin antibody as the profilin from pollen of the Europe
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