Identification and Characterization of Parietaria judaica Allergens

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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 chromato-focusing. 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.