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Valenta, R; Ball, T; Vrtala, S; Duchêne, M; Kraft, D; Scheiner, O.
cDNA cloning and expression of timothy grass (Phleum pratense) pollen profilin in Escherichia coli: comparison with birch pollen profilin.
Biochem Biophys Res Commun. 1994; 199(1):106-118 Doi: 10.1006/bbrc.1994.1201
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Co-authors Med Uni Graz: Ball Tanja
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Abstract:: Profilin, an actin-binding protein, was previously described as a ubiquitous allergen which is responsible for cross-reactivities in about 20% of pollen and food allergic patients. A complete cDNA clone coding for timothy grass (Phelum pratense) pollen profilin was isolated using allergic patients IgE. The deduced amino acid sequence of timothy grass profilin shares a sequence identity of 79% with birch profilin and other plant profilins and a lower average sequence identity of 35% with other eukaryotic profilins. The high degree of homology among different plant profilins at the DNA and protein level explains the extensive cross-reactivities observed in profilin allergic patients. Recombinant timothy grass pollen profilin was expressed in Escherichia coli as a beta-galactosidase fusion protein and shown to bind IgE from profilin allergic patients similar to recombinant birch profilin. Slight differences regarding the IgE-binding capacity of birch and timothy grass profilin indicate that not all IgE-epitopes of the two profilins are conserved. It is speculated that profilin allergic patients were initially sensitized against a certain profilin and then cross-react with the homologous proteins.
Find related publications in this database (using NLM MeSH Indexing): Allergens - genetics; Base Sequence -; Cloning, Molecular -; Contractile Proteins -; DNA, Complementary - genetics; Humans -; Immunoglobulin E - metabolism; Microfilament Proteins - genetics Microfilament Proteins - immunology; Molecular Sequence Data -; Poaceae -; Pollen -; Profilins -; Sequence Alignment -; Sequence Homology, Amino Acid -; Sequence Homology, Nucleic Acid -; Solubility -; Trees -