Oligomerization of profilins from birch, man and yeast. Profilin, a ligand for itself?

Irene Mittermann, Jacquelyn S. Fetrow, Diana L. Schaak, Steven C. Almo, Dietrich Kraft, Erwin Heberle-Bors, Rudolf Valenta

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Profilins are structurally well conserved low molecular weight (12-15 kDa) eukaryotic proteins which interact with a variety of physiological ligands: (1) cytoskeletal components, e.g., actin; (2) polyphosphoinositides, e.g., phosphatidylinositol-4,5-bisphosphate; (3) proline-rich proteins, e.g., formin homology proteins and vasodilatator-stimulated phosphoprotein. Profilins may thus link the microfilament system with signal transduction pathways. Plant profilins have recently been shown to be highly crossreactive allergens which bind to IgE antibodies of allergic patients and thus cause symptoms of type I allergy. We expressed and purified from Escherichia coli profilins from birch pollen (Betula verrucosa), humans (Homo sapiens) and yeast (Schizosaccharomyces pombe) and demonstrated that each of these profilins is able to form stable homo- and heteropolymers via disulphide bonds in vitro. Circular dichroism analysis of oxidized (polymeric) and reduced (monomeric) birch pollen profilin indicates that the two states have similar secondary structures. Using 125I-labeled birch pollen, yeast and human profilin in overlay experiments, we showed that disulphide bond formation between profilins can be disrupted under reducing conditions, while reduced as well as oxidized profilin states bind to actin and profilin-specific antibodies. Exposure of profilin to oxidizing conditions, such as when pollen profilins are liberated on the surface of the mucosa of atopic patients, may lead to profilin polymerization and thus contribute to the sensitization capacity of profilin as an allergen.

Original languageEnglish (US)
Pages (from-to)183-191
Number of pages9
JournalSexual Plant Reproduction
Volume11
Issue number4
DOIs
StatePublished - 1998

Fingerprint

Profilins
Betula
Yeasts
yeasts
Ligands
Pollen
pollen
disulfide bonds
allergens
profilins
oligomerization
ligands
Disulfides
Allergens
actin
Actins
circular dichroism spectroscopy
Phosphatidylinositol Phosphates
phosphoproteins
Proteins

Keywords

  • Cytoskeleton
  • Oligomerization
  • Pollen
  • Profilin
  • Type I allergy

ASJC Scopus subject areas

  • Plant Science

Cite this

Mittermann, I., Fetrow, J. S., Schaak, D. L., Almo, S. C., Kraft, D., Heberle-Bors, E., & Valenta, R. (1998). Oligomerization of profilins from birch, man and yeast. Profilin, a ligand for itself? Sexual Plant Reproduction, 11(4), 183-191. https://doi.org/10.1007/s004970050140

Oligomerization of profilins from birch, man and yeast. Profilin, a ligand for itself? / Mittermann, Irene; Fetrow, Jacquelyn S.; Schaak, Diana L.; Almo, Steven C.; Kraft, Dietrich; Heberle-Bors, Erwin; Valenta, Rudolf.

In: Sexual Plant Reproduction, Vol. 11, No. 4, 1998, p. 183-191.

Research output: Contribution to journalArticle

Mittermann, I, Fetrow, JS, Schaak, DL, Almo, SC, Kraft, D, Heberle-Bors, E & Valenta, R 1998, 'Oligomerization of profilins from birch, man and yeast. Profilin, a ligand for itself?', Sexual Plant Reproduction, vol. 11, no. 4, pp. 183-191. https://doi.org/10.1007/s004970050140
Mittermann, Irene ; Fetrow, Jacquelyn S. ; Schaak, Diana L. ; Almo, Steven C. ; Kraft, Dietrich ; Heberle-Bors, Erwin ; Valenta, Rudolf. / Oligomerization of profilins from birch, man and yeast. Profilin, a ligand for itself?. In: Sexual Plant Reproduction. 1998 ; Vol. 11, No. 4. pp. 183-191.
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