Identification and characterization of Parietaria judaica allergens.

Abstract

Allergens of Parietaria judaica pollen extract have been identified and characterized biochemically. Two main allergenic components, A1 and A2, have been found by crossed-radioimmunoelectrophoresis and demonstrated to be spread in a wide range of pH. Immunoblotting studies revealed that at least eight SDS-denatured polypeptides show IgE-binding activity. The one exhibiting the highest allergenic activity, named Pj10 (MW 10,000 daltons) was found in all the fractions when the pollen extract was fractionated by chromatofocusing. Bidimensional electrophoretic analysis suggested that Pj10 either can form homopolymeric proteins of different molecular weights or can be associated to a number of proteins by disulfide bridges. Furthermore, Pj10 is the main molecular structure with IgE-binding activity in the two allergenic components A1 and A2 defined by immunological criteria.