Expression of biologically recombinant human acidic fibroblast growth factor in Arabidopsis thaliana seeds via oleosin fusion technology.

The potential of oleosins to act as carriers for recombinant foreign proteins in plant cells has been established. Using the oleosin fusion technology, the protein can be targeted to oil bodies in oilseeds by fusing it to the N- or C-terminus of oleosin. In this study, aFGF was expressed in Arabidopsis thaliana seeds via oleosin fusion technology. A plant-preferred aFGF gene was synthesized by optimizing codon usage and was fused to the C-terminus of the A. thaliana 18.5kDa oleosin gene. The fusion gene was driven by the phaseolin promoter to confer seed-specific expression of the human acidic fibroblast growth factor in A. thaliana. The T-DNA region of the recombinant plasmid pKO-aFGF was introduced into the genome of Arabidopsis thaliana by the floral dip method. The aFGF protein expression was confirmed by SDS-PAGE and western blotting. The biological activity showed that oil bodies fused to aFGF stimulated NIH/3T3 cell proliferation activity.