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Development and Characterization of a Soybean Experimental Line Lacking the α′ Subunit of β‑Conglycinin and G1, G2, and G4 Glycinin
journal contribution
posted on 2017-12-11, 00:00 authored by Bo Song, Nathan W. Oehrle, Shanshan Liu, Hari B. KrishnanA soybean
experimental line (BSH-3) devoid of a subset of seed
storage proteins was developed by crossing a mutant donor line “HS99B”
with a Chinese cultivar “Dongnong47” (DN47). One-dimensional
and high-resolution 2-D gel electrophoresis revealed the absence of
G1 (A1aB2), G2 (A2B1a), and G4 (A5A4B3) glycinin and the
α′ subunit of β-conglycinin in BSH-3 seeds. Despite
the lack of these abundant seed proteins, BSH-3 seeds still accumulated
38% protein. BSH-3 seeds also accumulated high levels of free amino
acids as compared with DN47 seeds, particularly arginine, and the
amount of several essential amino acids were significantly elevated
in BSH-3 seeds. Elevated accumulation of α and β-subunit
of β-conglycinin, G5 glycinin, Kunitz trypsin inhibitor, and
Bowman-Birk protease inhibitor indicates seed proteome rebalancing
in BSH-3 seeds. Immunoblot analysis using sera from soybean allergic
patients demonstrated the complete lack of a major allergen (α′
subunit of β-conglycinin) in BSH-3 seeds. However, elevated
levels of other allergens were found in BSH-3 seeds due to proteome
rebalancing. Transmission electron microscopy observation of mature
seeds of BSH-3 revealed striking differences in the appearance of
the protein storage vacuoles when compared with DN47.