|Xu, Chenping - UNIVERSITY OF MARYLAND|
Submitted to: Plant Biology Annual Meeting
Publication Type: Abstract Only
Publication Acceptance Date: March 5, 2006
Publication Date: March 5, 2006
Citation: Natarajan, S.S., Xu, C., Caperna, T.J., Cregan, P.B., Bae, H., Garrett, W.M. 2006. Proteomic characterization of allergen proteins in sixteen soybean genotypes [abstract]. Plant Biology Annual Meeting 2006. August 05-09, Boston, MA. Abstract No. 32025. Technical Abstract: 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 [Gly m Bd 60K (alpha-subunit of beta-conglycinin /acidic and basic polypeptides of G2), Gly m Bd 30K, and Gly m Bd 28K], were observed among the different genotypes. In wild genotypes alpha-subunits of beta-conglycinin separated into 6 or 7 protein spots whereas 2-6 spots were evident in cultivated genotypes; all 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 1or 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 one ancestor genotype (PI 548362) that showed absence of this allergen. Major proteomic variation was observed between wild and cultivated soybean genotypes rather than among genotypes in the same group.