Biotech Updates

Scientists Devise a Novel Strategy for Purification of Recombinant Proteins Expressed in Plants

April 8, 2011

Plants have been perceived as an economical expression platform for the production of pharmaceutical proteins, such as vaccines and antibodies because of their low cost and unlimited scalability. However, transgenic plants produce only small amounts of foreign proteins, therefore an efficient purification system is essential. Reynal Tremblay of the University of Ontario, Canada, together with other scientists developed and characterized a novel strategy for purification of recombinant proteins in plants which is based on genetic fusion to soybean agglutinin (SBA), a sugar-binding protein.

They constructed an SBA fusion protein with reporting green fluorescent protein (GFP) and expressed it in Nicotina bethamiana plants. Over 2.5% total soluble protein (TSP) accumulation was observed in the leaves of the plants. Furthermore, the plant-derived fusion protein assembles to form tetramers which is important for its stability, maintains the capacity of SBA to cause cell agglutination, and the ability of GFP to floresce. The fusion protein can be rapidly recovered in yield more than 90% with high purity.

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