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 language | English |
|---|---|
| Pages (from-to) | 1383-1396 |
| Number of pages | 14 |
| Journal | Biological Chemistry |
| Volume | 383 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - Sep 1 2002 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Purification, structural and immunological characterization of a timothy grass (Phleum pratense) pollen allergen, Phl p 4, with cross-reactive potential
AU - Stumvoll, Sabina
AU - Lidholm, Jonas
AU - Thunberg, Ronald
AU - DeWitt, Asa Marknell
AU - Eibesteiner, Petra
AU - Swoboda, Ines
AU - Bugajska-Schretter, Agnes
AU - Spitzauer, Susanne
AU - Vangelista, Luca
AU - Kazemi-Shirazi, Lili
AU - Sperr, Wolfgang R.
AU - Valent, Peter
AU - Kraft, Dietrich
AU - Valenta, Rudolf
PY - 2002/9/1
Y1 - 2002/9/1
N2 - 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.
AB - 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.
KW - Allergy
KW - Circular dichroism spectroscopy
KW - Grass pollen allergen
KW - IgE cross-reactivity
KW - Phl p 4
UR - http://www.scopus.com/inward/record.url?scp=18644376280&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=18644376280&partnerID=8YFLogxK
U2 - 10.1515/BC.2002.157
DO - 10.1515/BC.2002.157
M3 - Article
VL - 383
SP - 1383
EP - 1396
JO - Biological Chemistry
JF - Biological Chemistry
SN - 1431-6730
IS - 9
ER -