Parietaria judaica flowering phenology, pollen production, viability and atmospheric circulation, and expansive ability in the urban environment: impacts of environmental factors.

Parietaria judaica (Urticaceae) grows abundantly in urban areas of the Mediterranean region. Its pollen is a major allergy source. We studied the species' distribution and abundance in and around Thessaloniki (Greece), pollen production and pollen season. We also examined how urban pollution affects pollen viability. Our ultimate goal was to obtain an estimate of the species' performance and ability to expand under different environmental conditions related to climate change. We mapped P. judaica and the other Urticaceae species. In a north- and a south-facing population, we recorded the progress of P. judaica flowering and estimated the pollen content per flower, shoot and surface unit. We concurrently assessed atmospheric circulation of Urticaceae pollen. We estimated P. judaica pollen viability and Cu, Pb and Zn concentrations in plants collected from sites differing in traffic intensity. P. judaica is the most abundant Urticaceae species in the area; its occurrence has increased dramatically over the last 100 years. Production of flowers is intense in spring and autumn. Flowering started 12 days earlier in the south-facing population in spring, and 3 days later in autumn. Pollen production was higher in spring and in the south-facing population. Flower and pollen production were positively correlated with the size of the plant and the flower, respectively. Copper and lead concentrations in plants were positively correlated with pollen viability, which was higher for plants collected from high-traffic sites. P. judaica has a high phenotypic plasticity; this is a feature that promotes success of expansive and invasive species. It is also well adapted to warm and polluted urban environments. The climatic change forecast for the Mediterranean region could provoke earlier, longer, and more pronounced flowering and, consequently, more P. judaica pollen in the air. In return, this would result in increased severity of Parietaria pollinosis.

Assignment of disulphide bridges in Par j 2.0101, a major allergen of Parietaria judaica pollen.

Par j 2.0101, a major allergen of the Parietaria judaica pollen, was expressed in E. coli, purified to homogeneity and fully characterised both at the structural and the functional level. The recombinant rPar j 2.0101 protein showed an allergenic activity in histamine release, skin prick tests and capacity to bind IgE, almost identical to that of the native allergens purified from aqueous pollen extract. The complete pattern of S-S bridges of rPar j 2.0101 was determined by enzymatic digestion with endoproteinase Lys-C followed by mass spectrometric analysis of the resulting peptide mixtures. The eight cysteines occurring in the allergenic protein were found to be paired into the following four disulphides: Cys35-Cys83, Cys45-Cys60, Cys61-Cys106 and Cys81-Cys121. This structural information probes Par j 2.0101 to attain a 3-D fold consistent with that of the non-specific lipid transfer protein (ns-LTP) family and it represents an effective molecular basis to develop modified antigens by selective site-directed mutagenesis for immunotherapy.

The allergens of Parietaria.

Parietaria is a genus of dicotyledonous weeds of the Urticaceae family including several species and its pollen grain is one of the most important allergenic sources in the Mediterranean area. Species belonging to this genus induce IgE responses in approximately 10 million people. Identification of allergens by means of independent strategies suggest that the allergens of the two more common species, Parietaria judaica and Parietaria Officinalis, show molecular weights ranging between 10 and 14 kD and that the allergens of the two extracts are highly cross-reactive. Biochemical analysis and molecular cloning allowed the isolation and immunological characterization of the two major allergens of the P. judaica pollen, Par j 1 and Par j 2. Sequence comparison suggests that the P j major allergens of P. Judaica belong to the nonspecific lipid transfer protein family, and three-dimensional modeling by homology has revealed that both proteins present a very conserved structural motif composed of four alpha-helices. Immunological analysis has shown that Par j 1 and Par j 2 are able to bind most of the P. Judaica-specific IgE and some of their IgE determinants have been mapped. Recombinant Par j 1 and Par j 2 allergens have been shown to possess immunological properties equivalent to their natural counterpart and their availability represents a fundamental tool for the diagnosis and therapy of Parietaria pollen allergy.