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Allergens from birch pollen and pollen of the European chestnut share common epitopes
Author(s) -
HIRSCHWEHR R.,
JÄGER S.,
HORAK F.,
FERREIRA F.,
VALENTA R.,
EBNER C.,
KRAFT D.,
SCHEINER O.
Publication year - 1993
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1993.tb00363.x
Subject(s) - profilin , pollen , allergen , epitope , immunoglobulin e , recombinant dna , monoclonal antibody , biology , allergy , antibody , immunology , microbiology and biotechnology , chemistry , botany , biochemistry , gene , actin cytoskeleton , cytoskeleton , cell
Summary Type I allergy to pollen of the European chestnut ( Castanea sativa ) represents a major cause of pollinosis in (sub) Mediterranean areas. Using sera from 14 patients with established allergy to pollen of the European chestnut, 13/14 sera (92%) showed IgE‐binding to a 22 kD protein, 2/14(14%) displayed additional binding to a 14 kD protein and 1/14 (7%) bound only to the 14 kD protein of European chestnut pollen extract. Two monoclonal mouse antibodies, BIP 1 and BIP 4, directed against different epitopes of Bet v I (the major birch pollen allergen), and a rabbit antibody to recombinant birch profilin (r Bet v II) were used to characterize the proteins of the European chestnut pollen. The recombinant birch pollen allergens, r Bet v I and r Bet v II (profilin) were employed to show common allergenic structures on proteins from both birch and European chestnut pollen by IgE‐inhibition experiments. Despite the fact that the 22 kD protein displayed a higher molecular weight in comparison to the 17 kD major birch pollen allergen, Bet v I, we could demonstrate reactivity of both monoclonal antibodies, BIP 1 and BIP 4, with this protein. A complete inhibiton of IgE‐binding to this 22 kD protein was shown by pre‐incubating sera with purified recombinant Set r I. In addition, the 14kD protein could be identified by IgE‐inhibition studies with recombinant Bet v II and by using a rabbit anti‐profilin antibody as the profilin from pollen of the European chestnut.