Purification and characterization of the major allergen from apple and its allergenic cross-reactivity with Bet v 1.
The major allergen from apple extract was concentrated by anion exchange chromatography and further purified by reverse-phase HPLC. A distinct peak with a high degree of homogeneity was obtained. The isolated protein has a MW of 18 kD and specific IgE-binding capacity (immunoblotting, IgE-binding inhibition). N-terminal amino acid analyses of the allergen allowed 37 cleavages and showed 67.6% identity to Bet v 1, the major allergen of birch pollen. Enzyme immunoassay inhibition studies with serum of birch/apple-allergic patients showed that besides cross-reacting structures to Bet v 1, apple-specific IgE antibodies could exist. Monoclonal antibodies (mAbs) were raised against the 18-kD allergen from apple and characterized by means of immunoblotting and ELISA. Only three of the eight studied mAbs reacted with Bet v 1.
Fahlbusch
B
B
Department of Clinical Immunology, University of Jena, Germany.
Rudeschko
O
O
Müller
W D
WD
Schlenvoigt
G
G
Vettermann
S
S
Jäger
L
L
D000485:Allergens / Q000276:immunology / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D003429:Cross Reactions; D005638:Fruit / Q000276:immunology*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology* / Q000302:isolation & purification; D011058:Pollen / Q000276:immunology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014197:Trees / Q000276:immunology*
D000485:Allergens; D052179:Antigens, Plant; D010940:Plant Proteins; C061312:Bet v 1 allergen, Betula