Enhanced expression of rabies virus surface G-protein in Escherichia coli using SUMO fusion

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

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)68-74
Number of pages7
JournalProtein Journal
Issue number1
StatePublished - Jan 2012


  • Animals
  • Escherichia coli/genetics
  • Gene Expression
  • Humans
  • Mice
  • Mice, Inbred BALB C
  • Rabies virus/genetics
  • Recombinant Fusion Proteins/genetics
  • Small Ubiquitin-Related Modifier Proteins/genetics
  • Viral Envelope Proteins/genetics

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't


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