A major allergen, the <i>Par j</i> I, was purified to homogeneity from <i>Parietaria judaica</i> pollen by means of ultrafiltration dialysis, preparative polyacrylamide gel chromatography and affinity chromatography through a column of Sepharose-monoclonal antibody specific for <i>Par j</i> I. The homogeneity of the <i>Par j</i> I was assessed by one single arc of immunoprecipitation both in crossed immunoelectrophoresis (CIE) and crossed radioimmunoelectrophoresis, by one single band of radiostaining after a sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transfer to nitrocellulose and by one single peak after a size exclusion chromatography on high-performance liquid chromatography (HPLC). The homogeneity was further supported by crossed Laurell immunoelectrophoretic analysis, in that only one arc of precipitation was magnified in CIE after addition of the purified allergen. The purified <i>Par j</i> I allergen was capable of interacting in vitro with 70% of the human IgE specific for a crude <i>P. judaica</i> extract, as determined by radioallergosorbent test inhibition. The purified <i>Par j</i> I was capable of inducing positive reactions in vivo in skin prick tests, and of inducing release of histamine from blood containing basophils as determined by a histamine release assay. The amino acid analysis of the <i>Par j</i> I showed 118 amino acid residues per monomer analyzed and, among other residues, three raethionine residues were detected. The molecular weight of the <i>Par j</i> I estimated by HPLC and amino acid composition was 26 kilodaltons.
Little is known about the pharmacokinetics of allergens for local immunotherapy. Thus, we studied the pharmacokinetics in allergic volunteers of a commercial allergenic vaccine in orosoluble tablets (LAIS ® , Lofarma S.p.A). The carbamylated monomeric allergoid derived from Parietaria judaica major allergen (Par j 1), characterized by maintenance of the original molecular size, and the native allergen, were radiolabelled with 123 I, then incorporated into the commercial soluble tablets and administered to allergic subjects. Early sequential and late static scintigraphic acquisitions were performed, and plasma radioactivity was measured at different time intervals. No difference in local pharmacokinetics was observed between the allergen and the allergoid: part of the tracer was retained in the mouth for at least 2 h after swallowing. No direct absorption through the oral mucosa could be detected, as plasma radioactivity increased only after swallowing and peaked at 2 h. However, the plasma peak attained with the allergoid in tablets was significantly higher with respect to the native allergen. Finally, some undegraded allergoid, but not the allergen, could be constantly detected in the bloodstream at plasma peak. The results showed a similar behaviour of the allergoid and the allergen in tablets as far as their local kinetics are concerned, whereas plasma peak was higher with the allergoid than with the allergen. Therefore we conclude that the chemical modification of the allergen may affect its pharmacokinetics, by making it less susceptible to enzymatic degradation.
The influence of age and sex has been in 208 asthmatic children on the basis of the following parameters: total serum IgE concentration (RIST), serum concentration of specific IgE antibodies (RAST), and positive prick tests against Dermatophagoides Pleronissynus, grasses, and Alternaria Tenuis. The results indicate that all these parameters are significantly influenced by age. Arithmetic values for RIST show a significant difference between the sexes which is obscured by logarithmic calculation. The data strongly suggest that IgE antibodies cannot be considered the main mechanism by which asthma is produced in small children.
The authors describe a clinical case of rhinitis and asthma in an angler after exposure to antigenic material released from larvae of fly, commonly used by anglers as bait. The common names of these larvae are "blue bottle", "green bottle" and "grey bottle". The patient was usually in good health, free from allergic diseases and free from asthmatic attacks when far from exposure to the baits. Spirometric evaluation revealed a fall of 21% in VEMS after challenge with antigen. Skin test (prick) with an extract obtained from the baits and RAST were strongly positive. By avoidance of exposure to antigen obtained changing type of bait, the asthmatic attacks completely disappeared. The authors discuss the clinical, diagnostic and preventive aspects of this allergic syndrome, and deal with the taxonomy of the insect.
Allergenic extracts ( Der p , grass, and Parietarin ) or single allergens such as Par j I (the major allergen of Parietaria ) and ovalbumin (OA), a food allergen widely used in animal models, were chemically modified by reaction with potassium cyanate (KCNO), which transforms the &‐amino group of the lysine of proteinaceous allergens into ureido groups. KCNO‐modified (carbamylated) allergens have low allergenic potency, as demonstrated in vitro (RAST inhibition) and in vivo (passive cutaneous anaphylaxis). When used to immunize rabbits, carbamylated allergens still induce IgG antibodies able to cross‐react with native allergens (immunoblotting experiments). An interesting feature distinguishing carbamylated allergens from other chemically modified allergens is the preservation of the native monomeric dimension as demonstrated by SDS‐PAGE analysis. Results are discussed from the perspective of clinical application of carbamylated allergens.
We studied a patient with rheumatoid arthritis (RA) and a high titer of IgE that could be attributed to a mono or oligoclonal expansion of IgE+ B lymphocytes. These IgE had no specificity for known allergens but bound to a panel of self (including Fc fragment of IgG) and exogenous antigens, displaying properties typical of polyspecific antibodies. We concluded that (1) RA can be associated with increased amounts of polyspecific IgE antibodies; (2) clonal excess populations of B cells are not a unique feature of malignant lymphoma, but may occur in autoimmune diseases in the form of a benign oligoclonal B cell proliferation.
