GST S. Japonicum

Glutathione S-Transferase (GST) from Schistosoma japonicum (SjGST) is a widely utilized enzyme in biochemical research and biotechnology. It is particularly known for its role as a fusion tag in the purification of recombinant proteins. This article delves into the background, structure, and applications of SjGST, with a focus on its recombinant form.

Schistosoma japonicum is a parasitic worm responsible for schistosomiasis, a significant health concern in many tropical regions. The GST enzyme from this organism has been extensively studied due to its unique properties. SjGST is a 26-kDa protein that forms homodimers . The crystal structure of non-fused SjGST complexed with glutathione has been determined, providing insights into its functional mechanisms .

Recombinant DNA technology has enabled the expression of SjGST in various host systems, such as Escherichia coli. This recombinant form retains the enzyme’s functional properties and is widely used in research. The recombinant SjGST can be fused to a protein of interest (POI), facilitating its purification through affinity chromatography using glutathione-immobilizing resins .

1. Protein Purification: The primary application of recombinant SjGST is in the purification of recombinant proteins. The GST-tag allows for efficient purification of POIs using commercially available glutathione-immobilizing resins .
2. Protein-Protein Interaction Studies: By fusing one member of the heterodimeric SjGST pair with a fluorescent protein and the other with the POI, researchers can conveniently and sensitively detect protein-protein interactions using fluorescence spectroscopy .
3. Vaccine Development: SjGST has also been explored as a potential vaccine candidate against schistosomiasis. Both native and recombinant forms of SjGST have shown promise in reducing worm burden and egg viability in experimental models .