Recombinant birch pollen allergens (rBet v 1 and rBet v 2) contain most of the IgE epitopes present in birch, alder, hornbeam, hazel, and oak pollen: a quantitative IgE inhibition study with sera from different populations.
BACKGROUND
Pollen from trees of the order Fagales are important allergen sources in most parts of the world. Clinical, immunochemical, and molecular biology studies indicate that they contain cross-reactive allergens. The major birch pollen allergen, Bet v 1, and birch profilin, Bet v 2, a highly cross-reactive allergen, have been cloned and expressed in Escherichia coli.


OBJECTIVE
The purpose of this study was to demonstrate the presence of allergens in Fagales pollens that share IgE epitopes with recombinant Bet v 1 and Bet v 2 and to determine the percentage of birch, alder, hornbeam, hazel, and oak pollen-specific IgE that can be preabsorbed with rBet v 1 and rBet v 2 from 102 sera of different populations of subjects allergic to Fagales tree pollen.


METHODS
The presence of rBet v 1- and rBet v 2-homologous allergens in tree pollen extracts was investigated by IgE immunoblot inhibition experiments, and the percentage of tree (birch, alder, hornbeam, hazel, and oak) pollen-specific IgE that was bound by a mixture of rBet v 1 and rBet v 2 was determined by RAST-based quantitative IgE inhibition experiments. The clinical significance of IgE antibody cross-reactivity was studied by skin prick testing with rBet v 1, rBet v 2, and Fagales pollen extracts.


RESULTS
Natural birch, alder, hornbeam, hazel, and oak pollen contain allergens that share IgE epitopes with rBet v 1 and rBet v 2. A combination of rBet v 1 and rBet v 2 accounted for 82% of tree pollen-specific IgE on average. Most of the tree pollen-specific IgE was directed against rBet v 1.


CONCLUSIONS
rBet v 1 and rBet v 2 contain most of the Fagales pollen-specific IgE epitopes and may therefore substitute natural tree pollen extracts not only for diagnosis but also for patient-tailored immunotherapy of tree pollen allergy.
Niederberger
V
V
Institute of Medical and Chemical Laboratory Diagnostics, AKH, University of Vienna, Austria.
Pauli
G
G
Grönlund
H
H
Fröschl
R
R
Rumpold
H
H
Kraft
D
D
Valenta
R
R
Spitzauer
S
S
D000328:Adult; D000485:Allergens / Q000737:chemistry / Q000276:immunology*; D052179:Antigens, Plant; D003285:Contractile Proteins; D003429:Cross Reactions; D018604:Epitope Mapping; D005260:Female; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D008297:Male; D008840:Microfilament Proteins / Q000737:chemistry / Q000276:immunology*; D008875:Middle Aged; D010936:Plant Extracts / Q000737:chemistry / Q000276:immunology; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology*; D011058:Pollen / Q000737:chemistry / Q000276:immunology*; D051304:Profilins; D011852:Radioallergosorbent Test; D011994:Recombinant Proteins / Q000737:chemistry / Q000276:immunology; D012882:Skin Tests; D014197:Trees
D000485:Allergens; D052179:Antigens, Plant; D003285:Contractile Proteins; D008840:Microfilament Proteins; D010936:Plant Extracts; D010940:Plant Proteins; D051304:Profilins; D011994:Recombinant Proteins; C061312:Bet v 1 allergen, Betula; D007073:Immunoglobulin E