Beschreibung:
<jats:title>Abstract</jats:title><jats:p>The weed wall pellitory, <jats:italic>Parietaria judaica</jats:italic>, is one the most important pollen allergen sources in the Mediterranean area causing severe symptoms of hay fever and asthma in allergic patients. We report the expression of the major <jats:italic>Parietaria</jats:italic> allergens, Par j 1 and Par j 2 which belong to the family of lipid transfer proteins, in insect cells. According to circular dichroism analysis and gel filtration, the purified allergens represented folded and monomeric proteins. Insect cell-expressed, folded Par j 2 exhibited higher IgE binding capacity and more than 100-fold higher allergenic activity than unfolded <jats:italic>Escherichia coli</jats:italic>-expressed Par j 2 as demonstrated by IgE ELISA and basophil activation testing. IgE ELISA inhibition assays showed that Par j 1 and Par j 2, contain genuine and cross-reactive IgE epitopes. IgG antibodies induced by immunization with Par j 2 inhibited binding of allergic patients IgE to Par j 1 only partially. IgE inhibition experiments demonstrated that insect cell-expressed Par j 1 and Par j 2 together resembled the majority of allergenic epitopes of the <jats:italic>Parietaria</jats:italic> allergome and therefore both should be used for molecular diagnosis and the design of vaccines for allergen-specific immunotherapy of <jats:italic>Parietaria</jats:italic> allergy.</jats:p>