A novel expression system for production of soluble prion proteins in E. coli.

TitleA novel expression system for production of soluble prion proteins in E. coli.
Publication TypeJournal Article
Year of Publication2012
AuthorsAbskharon, R. N. N., S. Ramboarina, H. El Hassan, W. Gad, M. I. Apostol, G. Giachin, G. Legname, J. Steyaert, J. Messens, S. H. Soror, and A. Wohlkonig
JournalMicrob Cell Fact
Date Published2012 Jan 10
KeywordsBiotechnology, Escherichia coli, Genetic Vectors, Humans, Oxidoreductases Acting on Sulfur Group Donors, Prions, Protein Disulfide Reductase (Glutathione), Protein Folding, Protein Structure, Tertiary, Recombinant Proteins

Expression of eukaryotic proteins in Escherichia coli is challenging, especially when they contain disulfide bonds. Since the discovery of the prion protein (PrP) and its role in transmissible spongiform encephalopathies, the need to obtain large quantities of the recombinant protein for research purposes has been essential. Currently, production of recombinant PrP is achieved by refolding protocols. Here, we show that the co-expression of two different PrP with the human Quiescin Sulfhydryl OXidase (QSOX), a human chaperone with thiol/disulfide oxidase activity, in the cytoplasm of E. coli produces soluble recombinant PrP. The structural integrity of the soluble PrP has been confirmed by nuclear magnetic resonance spectroscopy, demonstrating that properly folded PrP can be easily expressed in bacteria. Furthermore, the soluble recombinant PrP produced with this method can be used for functional and structural studies.

Alternate JournalMicrob. Cell Fact.
PubMed ID22233534
PubMed Central IDPMC3283519
Research group: