Submitted to: Mid Atlantic Plant Molecular Biology Society Conference
Publication Type: Abstract Only
Publication Acceptance Date: June 25, 2006
Publication Date: August 17, 2006
Citation: Natarajan, S.S., Xu, C., Caperna, T.J., Cregan, P.B., Bae, H., Garrett, W.M. 2006. Characterization of major allergen proteins of soybean by proteomic tools. Mid Atlantic Plant Molecular Biology Society Conference 2006. August 17-18, 2006. Beltsville MD. Abstract #11. .
We investigated profiles of three major allergen proteins (Gly m Bd 60K, Gly m Bd 30K and Gly m Bd 28K) in sixteen different soybean genotypes that included four groups; wild, cultivated, modern (elite), and ancestor. Four genotypes were studied within each group. All allergen proteins were well separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and characterized using mass spectrometry. Variation in the overall appearance and distribution patterns of allergen proteins were observed among the different genotypes. In wild genotypes the '-subunits of '-conglycinin separated into 6 or 7 protein spots whereas only 2-6 spots were evident in cultivated genotypes. Genotypes of modern and ancestor groups showed 2-5 protein spots. In contrast, glycinin G2 acidic polypeptide showed 4-5 spots in all genotypes. The G2 basic polypeptide showed 1-3 spots in wild, compared to 2 spots in cultivated, modern and ancestor soybean genotypes. One protein spot was detected for Gly m Bd 30K/P34 in wild compared to 1 or 2 spots in cultivated and 2 spots in other genotypes. Two protein spots were detected for Gly m Bd 28K in all genotypes except one modern genotype (PI 513382) that had one protein spot and no allergen spot was detected in one of the ancestor genotype (PI 548362). Major proteomic variation was observed between wild and cultivated soybean genotypes rather than among genotypes in the same group.