2010 Volume 16 Issue 4 Pages 341-346
Many allergens belong to the defense response proteins, which are produced when the plant is under various stresses. The amino acid sequences of the main wheat flour allergens associated with baker's asthma were analyzed in this study. The gene sequences of monomeric (WMAI), dimeric (WDAI), tetrameric (WTAI, which contains 1 WTAI-CM2 unit, 2 CM3 units and 1 CM16 unit) α-amylase inhibitor and fructose bisphosphate aldolase from wheat, barley and rye were obtained and characterized. Compared with other main allergens, it was shown that the fifteen proteins have a common conserved cysteine skeleton and the presence of CC and CX1-4C motifs, which are not usually found in other non-allergenic proteins. Most of these allergens have putative N-glycosylation sites. Protein structure either mediated through di-sulfide bonds or through higher order protein-protein interactions, plays a critical role in the allergenicity of allergens. It was also found that the same protein family allergens did not share similar 3D structures. With regard to the characterized sequences as well as protein structures of allergens, it is obvious that the flour proteins that have been implicated as important wheat seed allergens causing baker's asthma are complex but have some specific related behavioral traits.
