SearchPublisher and Institutes
You are here: Home :: Area NEM :: Life sciences :: Biochemistry
S. Stumvoll, J. Lidholm, R. Thunberg, A. M. DeWitt, P. Eibensteiner, I. Swoboda, A. Bugajska-Schretter, S. Spitzauer, L. Vangelista, L. Kazemi-Shirazi, W.R. Sperr, P. Valent, D. Kraft, R. Valenta
Purification, Structural and Immunological Characterization of a Timothy Grass (Phleum pratense) Pollen Allergen, Phl p 4, with Cross-Reactive Potential
Almost 500 million people worldwide suffer from Type I allergy, a genetically determined immunodisorder which is based on the production of IgE antibodies against per se harmless antigens (allergens). Due to their worldwide distribution and heavy pollen production, grasses represent a major allergen source for approximately 40% of allergic patients. We purified Phl p 4, a major timothy grass (Phleum pratense) pollen allergen with a molecular mass of 61.3 kDa and a pI of 9.6 to homogeneity. Circular dichroism spectroscopical analysis indicates that Phl p 4 contains a mixed ?helical/?pleated secondary structure and, unlike many other allergens, showed no reversible unfolding after thermal denaturation. We show that Phl p 4 is a major allergen which reacts with IgE antibodies of 75% of grass pollen allergic patients (n=150) and induces basophil histamine release as well as immediate type skin reactions in sensitized individuals. Phl p 4-specific IgE from three patients as well as two rabbitanti Phl p 4 antisera crossreacted with allergens present in pollen of trees, grasses, weeds as well as plantderived food. Rabbit antibodies raised against Phl p 4 also inhibited the binding of allergic patients IgE to Phl p 4. Phl p 4 may thus be used for diagnosis and treatment of sensitized allergic patients.
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 383, 09/2002
Pages: 1383 - 1396