Measurement of IgE antibodies against purified grass-pollen allergens (Ph1 p 1, 2, 3, 4, 5, 6, 7, 11, and 12) in sera of patients allergic to grass pollen

Background: Current allergy diagnosis is performed with allergen extracts which contain a variety of allergenic and nonallergenic components. The availability of highly purified and well-characterized allergen molecules seems to be an advantage of component-based diagnosis. Methods: With the immunoenzymatic CAP FEIA System. we measured specific IgE levels to the recombinant allergens rPhl p 1, rPhl p 2, rPhl p 5, rPhl p 6. rPhl p 7, rPhl p 11, rPhl p 12, and native Phl p 4 in 77 sera of patients allergic to grass pollen, in order to evaluate the IgE-binding frequency to these purified grass-pollen allergens and their relationship to rBet v 4, rBet v 2, and other allergens. Results: The frequency of sensitization was as follows: rPhl p 1 = 93.5%; rPhl p 2 = 67.5%; rPhl p 5 = 72.7%; rPhl p 6 = 68.8%; rPhl p 7 = 7.8%, rPhl p 11 = 53.2%; rPhl p 12 = 35.1%; and native Phl p 4 = 88.3%. As expected, rPhl p 7 and rPhl p 12 had a very good correlation (Spearman's r) with Bet v 4 (r = 0.95%, P < 0.05) and rBet v 2 (r = 0.99, P < 0.05), respectively. Good correlations of rPhl p 12 with papain (r = 0.93. P < 0.05), latex (r = 0.92. P < 0.05), and bromelain (r = 0.86, P < 0.05) were found. Highly variable individual sensitization patterns were observed. Conclusions: A new clinical approach has allowed the determination of specific allergograms for the different patients and may therefore be of great importance for more specific diagnosis. The use of component-resolved diagnostics may be useful to evaluate the allergen content of an extract for immunotherapy by monitoring patient's IgE and IgG directed to relevant allergens.