Background Plants of the genus Parietaria, Urticaceae family, represent a major cause of pollinosis in the Mediterranean area. Different Parietaria species crossreuct to a great extent, but studies on the crossreactivity among the major allergens of these pollens have not been carried out so far.
Objective To develop an immunochemical method to quantify the major Parieiarin judaica allergen. Par j 1, as well as to verify the presence of Par j 1-like proteins in different Urticaceae pollens. These proteins would be purified in order to study the cross-reactivity among them.
Methods Immunoaffinity chromatography with a monoclonal antibody, solid-phase enzyme-linked immunoassays and SDS-PAGE.
Results A monoclonal antibody-based ELISA for the quantisation of Par j 1 has been developed. The assay has a sensitivity of 0.2 ng/mL and shows a high correlation with the allergenic activity of P. judaica extracts determined by radioallergosorbent assay (RAST) inhibition.
By means of this assay, proteins homologous to Par j I were detected in P. officinalis and P. mauritanica. These proteins (Par o 1 and Par m 1, respectively) were purified by affinity chromatography using the same monoclomal antibody employed in the ELISA. Crossed-inhibition experiments demonstrated that Par j 1. Par o 1. and Par m 1, competed for the binding of specific IgE from a P. judaica-sensitive patients serum pool.
Conclusion The results here described suggest that shared allergenic epitopes are present in the three main allergens investigated, which may simplify the diagnosis and therapy for Parietaria allergy.