Details

Autor(en) / Beteiligte

• Liaw, Shwu-Huey
• Lee, Donna Y.
• Chow, Liu-Ping
• Lau, Gai-Xuong
• Su, Song-Nan

Titel

Structural Characterization of the 60-kDa Bermuda Grass Pollen Isoallergens, a Covalent Flavoprotein

Ist Teil von

• Biochemical and biophysical research communications, 2001-01, Vol.280 (3), p.738-743

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2001

Quelle

Access via ScienceDirect (Elsevier)

Beschreibungen/Notizen

• 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°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 (∼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.