Purification, structural and immunological characterization of a timothy grass (Phleum pratense) pollen allergen, Phl p 4, with cross-reactive potential

Sabina Stumvoll, Jonas Lidholm, Ronald Thunberg, Asa Marknell DeWitt, Petra Eibesteiner, Ines Swoboda, Agnes Bugajska-Schretter, Susanne Spitzauer, Luca Vangelista, Lili Kazemi-Shirazi, Wolfgang R. Sperr, Peter Valent, Dietrich Kraft, Rudolf Valenta

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

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 pl of 9.6 to homogeneity. Circular dichroism spectroscopical analysis indicates that Phl p 4 contains a mixed α-helical/β-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 rabbit-anti Phl p 4 antisera cross-reacted with allergens present in pollen of trees, grasses, weeds as well as plant-derived 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.

Original languageEnglish
Pages (from-to)1383-1396
Number of pages14
JournalBiological Chemistry
Volume383
Issue number9
DOIs
Publication statusPublished - Sep 1 2002
Externally publishedYes

Fingerprint

Phleum
Pollen
Allergens
Purification
Immunoglobulin E
Poaceae
Antibodies
Rabbits
Allergies
Edible Plants
Denaturation
Basophils
Histamine Release
Molecular mass
Circular Dichroism
Histamine
Antibody Formation
Phleum pratense Phl p 4 protein
Immune Sera
Skin

Keywords

  • Allergy
  • Circular dichroism spectroscopy
  • Grass pollen allergen
  • IgE cross-reactivity
  • Phl p 4

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification, structural and immunological characterization of a timothy grass (Phleum pratense) pollen allergen, Phl p 4, with cross-reactive potential. / Stumvoll, Sabina; Lidholm, Jonas; Thunberg, Ronald; DeWitt, Asa Marknell; Eibesteiner, Petra; Swoboda, Ines; Bugajska-Schretter, Agnes; Spitzauer, Susanne; Vangelista, Luca; Kazemi-Shirazi, Lili; Sperr, Wolfgang R.; Valent, Peter; Kraft, Dietrich; Valenta, Rudolf.

In: Biological Chemistry, Vol. 383, No. 9, 01.09.2002, p. 1383-1396.

Research output: Contribution to journalArticle

Stumvoll, S, Lidholm, J, Thunberg, R, DeWitt, AM, Eibesteiner, P, Swoboda, I, Bugajska-Schretter, A, Spitzauer, S, Vangelista, L, Kazemi-Shirazi, L, Sperr, WR, Valent, P, Kraft, D & Valenta, R 2002, 'Purification, structural and immunological characterization of a timothy grass (Phleum pratense) pollen allergen, Phl p 4, with cross-reactive potential', Biological Chemistry, vol. 383, no. 9, pp. 1383-1396. https://doi.org/10.1515/BC.2002.157
Stumvoll, Sabina ; Lidholm, Jonas ; Thunberg, Ronald ; DeWitt, Asa Marknell ; Eibesteiner, Petra ; Swoboda, Ines ; Bugajska-Schretter, Agnes ; Spitzauer, Susanne ; Vangelista, Luca ; Kazemi-Shirazi, Lili ; Sperr, Wolfgang R. ; Valent, Peter ; Kraft, Dietrich ; Valenta, Rudolf. / Purification, structural and immunological characterization of a timothy grass (Phleum pratense) pollen allergen, Phl p 4, with cross-reactive potential. In: Biological Chemistry. 2002 ; Vol. 383, No. 9. pp. 1383-1396.
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