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Almost 500 million people worldwide suffer from TypeI allergy, a genetically determined immunodisorder which is based on theproduction of IgE antibodies against per se harmless antigens (allergens). Dueto their worldwide distribution and heavy pollen production, grasses representa major allergen source for approximately 40% of allergic patients. We purifiedPhl p 4, a major timothy grass (Phleum pratense) pollen allergen with amolecular mass of 61.3 kDa and a pI of 9.6 to homogeneity. Circular dichroismspectroscopical analysis indicates that Phl p 4 contains a mixedαhelical/βpleated secondary structure and, unlike many other allergens, showedno reversible unfolding after thermal denaturation. We show that Phl p 4 is amajor allergen which reacts with IgE antibodies of 75% of grass pollen allergicpatients (n=150) and induces basophil histamine release as well as immediatetype skin reactions in sensitized individuals. Phl p 4-specific IgE from threepatients as well as two rabbitanti Phl p 4 antisera crossreacted with allergenspresent in pollen of trees, grasses, weeds as well as plantderived food. Rabbitantibodies raised against Phl p 4 also inhibited the binding of allergicpatients IgE to Phl p 4. Phl p 4 may thus be used for diagnosis and treatmentof sensitized allergic patients.

biological chemistry

Purification, Structural and Immunological     Characterization of a Timothy Grass (Phleum pratense) Pollen Allergen, Phl p 4,     with Cross-Reactive Potential