Expression of a functional recombinant oleosin-human hyaluronidase hPH-20 fusion in Arabidopsis thaliana.

Abstract The use of plants as expression systems for the production of recombinant proteins has distinct advantages, such as safety, ease, low cost and high yields. A plant binary expression vector, pOTBar-hPH20, containing an oleosin-hPH20 fusion gene and a Basta selection marker gene was constructed and introduced into Arabidopsis thaliana via the floral dip method. Transformed A. thalian a seed lines were obtained and analyzed by PCR. The PCR results indicated that oleosin-hPH20 fusion gene was integrated into the A. thalian a genome. The oleosin-hPH20 fusion protein was detected by SDS–PAGE and Western blot analysis. The oleosin-hPH20 fusion protein was expressed and had good antigenicity in the transgenic A. thaliana seeds. An enzyme assay suggested that the recombinant oleosin-hPH20 fusion protein had hyaluronidase activity.