flavin-adenine-dinucleotide and Rhinitis--Allergic--Seasonal

Our studies suggest a tripartite structure for the 60-kDa allergen of Bermuda grass pollen (BG60) including a short N-terminal segment, a FAD-binding domain, and a C-terminal domain. The lower molecular weight isoallergens lack the N-terminal segment. The higher protease susceptibility and the lower melting temperature of approximately 20 degrees C of the lower molecular weight isoforms suggest that the N-terminal segment is essential for a compact structure. Database screening reveals that the protease-digested peptide sequences (approximately 180 residues in total) share 40% identity with the plant berberine bridge enzymes. In particular, a 24-residue peptide sequence displays high similarity to a conserved FAD-binding motif. The spectroscopic and SDS-PAGE analyses suggest that the cofactor FAD is covalently linked to the central domain. Therefore, we conclude that BG60 is identified as the first flavinylated allergen.

Topics: Allergens; Amino Acid Sequence; Binding Sites; Flavin-Adenine Dinucleotide; Flavoproteins; Humans; Metals; Molecular Sequence Data; Molecular Weight; Plant Proteins; Poaceae; Pollen; Protein Structure, Tertiary; Rhinitis, Allergic, Seasonal; Sequence Homology, Amino Acid