Journal
PROTEIN JOURNAL
Volume 31, Issue 1, Pages 68-74Publisher
SPRINGER
DOI: 10.1007/s10930-011-9373-6
Keywords
Enhanced expression; Rabies glycoprotein; Recombinant protein; Solubility; SUMO fusion
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Funding
- Council of Scientific and Industrial Research (CSIR), New Delhi, India
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Fusion systems are known to increase the expression of difficult to express recombinant proteins in soluble form to facilitate their purification. Rabies glycoprotein was also tough to express at sufficient level in soluble form in both E. coli and plant. The present work was aimed to over-express and purify this membrane protein from soluble extract of E. coli. Fusion of Small Ubiqutin like Modifier (SUMO) with rabies glycoprotein increased similar to 1.5 fold higher expression and similar to 3.0 fold solubility in comparison to non-fused in E. coli. The SUMO fusion also simplified the purification process. Previously engineered rabies glycoprotein gene in tobacco plants provides complete protection to mice, but the expression was very low for purification. Our finding demonstrated that the SUMO-fusion was useful for enhancing expression and solubility of the membrane protein and again proves to be a good alternative technology for applications in biomedical and pharmaceutical research.
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