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Licensed Unlicensed Requires Authentication Published by De Gruyter June 1, 2005

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

  • 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 and R. Valenta
From the journal Biological Chemistry


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 αhelical/βpleated 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.

Published Online: 2005-06-01
Published in Print: 2002-09-17

Copyright © 2002 by Walter de Gruyter GmbH & Co. KG

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