Enhanced Expression of Rabies Virus Surface G-Protein in Escherichia coli using SUMO Fusion View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-12-02

AUTHORS

Ankit Singh, Dinesh Yadav, Krishan Mohan Rai, Meenal Srivastava, Praveen C. Verma, Pradhyumna K. Singh, Rakesh Tuli

ABSTRACT

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 ~1.5 fold higher expression and ~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. More... »

PAGES

68-74

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10930-011-9373-6

DOI

http://dx.doi.org/10.1007/s10930-011-9373-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014482769

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22134654


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