IgE binding to a new cross-reactive structure: a 35 kDa protein in birch pollen, exotic fruit and other plant foods.
Wellhausen A., Schöning B., Petersen A., Vieths S.
Author Affiliation: Forschungszentrum Borstel, Division of Allergology, 23845 Borstel, Germany.
Zeitschrift für Ernährungswissenschaft 35 : 348-355
Abstract : A new cross-reactive structure of 35 kDa was identified in birch pollen and some plant food extracts by enzyme allergosorbent test (EAST) and immunoblot inhibition studies. The 35 kDa birch pollen protein is a minor allergen to which approximately 10-15% of birch pollen allergic individuals have specific IgE. These data demonstrate that there is cross-reactivity of this protein with proteins of comparable size from lychee, mango, banana, orange, apple, pear and carrot. While the 35 kDa protein is immunologically independent of the major birch pollen allergen Bet v 1, IgE binding was also observed to a 34 kDa structure which seemed to be a Bet v 1 dimer.