Calcium-dependent immunoglobulin E recognition of the apo- and calcium- bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7

Verena Niederberger, Brigitte Hayek, Susanne Vrtala, Sylvia Laffer, Anna Twardosz, Luca Vangelista, Wolfgang R. Sperr, Peter Valent, Helmut Rumpold, Dietrich Kraft, Klaus Ehrenberger, Rudolf Valenta, Susanne Spitzauer

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

Type I allergy, an immunodisorder that affects almost 20% of the population worldwide, is based on the immunoglobulin E (IgE) recognition of per se innocuous antigens (allergens). Pollen from wind-pollinated plants belong to the most potent allergen sources. We report the isolation of a cDNA coding for a 8.6 kDa two EF-hand calcium binding allergen, Phl p 7, from a timothy grass (Phleum pratense) pollen expression cDNA library, using serum IgE from a grass pollen allergic patient. Sequence analysis identified Phl p 7 as a member of a recently discovered subfamily of pollen-specific calcium binding proteins. Recombinant Phl p 7 was expressed in Escherichia coli and purified to homogeneity as determined by mass spectroscopy. Approximately 10% of pollen allergic patients displayed IgE reactivity to rPhl p 7 and Phl p 7- homologous allergens present in pollens of monocotyledonic and dicotyledonic plants. Circular dichroism analysis of the calcium-bound and apo-rPhl p 7 indicated that differences in IgE recognition may be due to calcium-induced changes in the protein conformation. The fact that patients mount IgE antibodies against different protein conformations is interpreted as a footprint of a preferential sensitization against either form. The biological activity of rPhl p 7 was demonstrated by its ability to induce basophil histamine release and immediate type skin reactions in sensitized individuals. In conclusion, IgE binding to Phl p 7 represents an example for the conformation-dependent IgE recognition of an allergen. Recombinant Phl p 7 may be used for diagnosis and perhaps treatment of a group of patients who suffer from allergy to pollens of many unrelated plant species.

Original languageEnglish
Pages (from-to)843-856
Number of pages14
JournalFASEB Journal
Volume13
Issue number8
Publication statusPublished - 1999
Externally publishedYes

Fingerprint

Phleum
EF Hand Motifs
immunoglobulin E
Phleum pratense
Pollen
allergens
Immunoglobulin E
hands
pollen
Calcium
calcium
Allergens
Allergies
Conformations
protein conformation
Protein Conformation
hypersensitivity
circular dichroism spectroscopy
calcium-binding proteins
basophils

Keywords

  • Allergen
  • Circular dichroism spectroscopy
  • Conformational epitopes
  • Cross-reactivity
  • EF-hand protein
  • Pollen-specific expression
  • Type I allergy

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Calcium-dependent immunoglobulin E recognition of the apo- and calcium- bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. / Niederberger, Verena; Hayek, Brigitte; Vrtala, Susanne; Laffer, Sylvia; Twardosz, Anna; Vangelista, Luca; Sperr, Wolfgang R.; Valent, Peter; Rumpold, Helmut; Kraft, Dietrich; Ehrenberger, Klaus; Valenta, Rudolf; Spitzauer, Susanne.

In: FASEB Journal, Vol. 13, No. 8, 1999, p. 843-856.

Research output: Contribution to journalArticle

Niederberger, V, Hayek, B, Vrtala, S, Laffer, S, Twardosz, A, Vangelista, L, Sperr, WR, Valent, P, Rumpold, H, Kraft, D, Ehrenberger, K, Valenta, R & Spitzauer, S 1999, 'Calcium-dependent immunoglobulin E recognition of the apo- and calcium- bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7', FASEB Journal, vol. 13, no. 8, pp. 843-856.
Niederberger, Verena ; Hayek, Brigitte ; Vrtala, Susanne ; Laffer, Sylvia ; Twardosz, Anna ; Vangelista, Luca ; Sperr, Wolfgang R. ; Valent, Peter ; Rumpold, Helmut ; Kraft, Dietrich ; Ehrenberger, Klaus ; Valenta, Rudolf ; Spitzauer, Susanne. / Calcium-dependent immunoglobulin E recognition of the apo- and calcium- bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. In: FASEB Journal. 1999 ; Vol. 13, No. 8. pp. 843-856.
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abstract = "Type I allergy, an immunodisorder that affects almost 20{\%} of the population worldwide, is based on the immunoglobulin E (IgE) recognition of per se innocuous antigens (allergens). Pollen from wind-pollinated plants belong to the most potent allergen sources. We report the isolation of a cDNA coding for a 8.6 kDa two EF-hand calcium binding allergen, Phl p 7, from a timothy grass (Phleum pratense) pollen expression cDNA library, using serum IgE from a grass pollen allergic patient. Sequence analysis identified Phl p 7 as a member of a recently discovered subfamily of pollen-specific calcium binding proteins. Recombinant Phl p 7 was expressed in Escherichia coli and purified to homogeneity as determined by mass spectroscopy. Approximately 10{\%} of pollen allergic patients displayed IgE reactivity to rPhl p 7 and Phl p 7- homologous allergens present in pollens of monocotyledonic and dicotyledonic plants. Circular dichroism analysis of the calcium-bound and apo-rPhl p 7 indicated that differences in IgE recognition may be due to calcium-induced changes in the protein conformation. The fact that patients mount IgE antibodies against different protein conformations is interpreted as a footprint of a preferential sensitization against either form. The biological activity of rPhl p 7 was demonstrated by its ability to induce basophil histamine release and immediate type skin reactions in sensitized individuals. In conclusion, IgE binding to Phl p 7 represents an example for the conformation-dependent IgE recognition of an allergen. Recombinant Phl p 7 may be used for diagnosis and perhaps treatment of a group of patients who suffer from allergy to pollens of many unrelated plant species.",
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T1 - Calcium-dependent immunoglobulin E recognition of the apo- and calcium- bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7

AU - Niederberger, Verena

AU - Hayek, Brigitte

AU - Vrtala, Susanne

AU - Laffer, Sylvia

AU - Twardosz, Anna

AU - Vangelista, Luca

AU - Sperr, Wolfgang R.

AU - Valent, Peter

AU - Rumpold, Helmut

AU - Kraft, Dietrich

AU - Ehrenberger, Klaus

AU - Valenta, Rudolf

AU - Spitzauer, Susanne

PY - 1999

Y1 - 1999

N2 - Type I allergy, an immunodisorder that affects almost 20% of the population worldwide, is based on the immunoglobulin E (IgE) recognition of per se innocuous antigens (allergens). Pollen from wind-pollinated plants belong to the most potent allergen sources. We report the isolation of a cDNA coding for a 8.6 kDa two EF-hand calcium binding allergen, Phl p 7, from a timothy grass (Phleum pratense) pollen expression cDNA library, using serum IgE from a grass pollen allergic patient. Sequence analysis identified Phl p 7 as a member of a recently discovered subfamily of pollen-specific calcium binding proteins. Recombinant Phl p 7 was expressed in Escherichia coli and purified to homogeneity as determined by mass spectroscopy. Approximately 10% of pollen allergic patients displayed IgE reactivity to rPhl p 7 and Phl p 7- homologous allergens present in pollens of monocotyledonic and dicotyledonic plants. Circular dichroism analysis of the calcium-bound and apo-rPhl p 7 indicated that differences in IgE recognition may be due to calcium-induced changes in the protein conformation. The fact that patients mount IgE antibodies against different protein conformations is interpreted as a footprint of a preferential sensitization against either form. The biological activity of rPhl p 7 was demonstrated by its ability to induce basophil histamine release and immediate type skin reactions in sensitized individuals. In conclusion, IgE binding to Phl p 7 represents an example for the conformation-dependent IgE recognition of an allergen. Recombinant Phl p 7 may be used for diagnosis and perhaps treatment of a group of patients who suffer from allergy to pollens of many unrelated plant species.

AB - Type I allergy, an immunodisorder that affects almost 20% of the population worldwide, is based on the immunoglobulin E (IgE) recognition of per se innocuous antigens (allergens). Pollen from wind-pollinated plants belong to the most potent allergen sources. We report the isolation of a cDNA coding for a 8.6 kDa two EF-hand calcium binding allergen, Phl p 7, from a timothy grass (Phleum pratense) pollen expression cDNA library, using serum IgE from a grass pollen allergic patient. Sequence analysis identified Phl p 7 as a member of a recently discovered subfamily of pollen-specific calcium binding proteins. Recombinant Phl p 7 was expressed in Escherichia coli and purified to homogeneity as determined by mass spectroscopy. Approximately 10% of pollen allergic patients displayed IgE reactivity to rPhl p 7 and Phl p 7- homologous allergens present in pollens of monocotyledonic and dicotyledonic plants. Circular dichroism analysis of the calcium-bound and apo-rPhl p 7 indicated that differences in IgE recognition may be due to calcium-induced changes in the protein conformation. The fact that patients mount IgE antibodies against different protein conformations is interpreted as a footprint of a preferential sensitization against either form. The biological activity of rPhl p 7 was demonstrated by its ability to induce basophil histamine release and immediate type skin reactions in sensitized individuals. In conclusion, IgE binding to Phl p 7 represents an example for the conformation-dependent IgE recognition of an allergen. Recombinant Phl p 7 may be used for diagnosis and perhaps treatment of a group of patients who suffer from allergy to pollens of many unrelated plant species.

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KW - Circular dichroism spectroscopy

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