Oxidative Folding of Proteins in Escherichia Coli - The author highlights novel strains and methods that have recently been shown to express multidisulfide bonded proteins. This article is part of a s

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Oxidative Folding of Proteins in Escherichia Coli
The author highlights novel strains and methods that have recently been shown to express multidisulfide bonded proteins. This article is part of a special section on expression systems.


BioPharm International
Volume 25, Issue 5, pp. 48-54

CONCLUSION

It has been two decades since the discovery of enzymes responsible for the formation of disulfide bonds in E. coli (61). Although great progress in understanding the molecular mechanism of disulfide bond formation has been made, comparatively little progress has been achieved in engineering novel strains which can correctly express multidisulfide bonded proteins. This lack of progress is mainly due to the fact that a given solution for expressing a recombinant protein is usually not transferable to the next protein. Thus, for each protein the researcher must start from scratch to find the suitable expression strain and condition.

One bottleneck for the researcher is the limited number of strains available to express disulfide bonded proteins. Those few new strains along with tools and techniques to assist the researcher in expressing disulfide bonded proteins have been reviewed here. The author hopes that increased molecular understanding of disulfide bond formation will result in an increasing repertoire of novel strains that are capable of producing active soluble recombinant proteins.

MEHMET BERKMEN, PHD, is a staff scientist at New England Biolabs, 240 County RD, Ipswich, MA 01938-2723, tel. 978.380.7519,
.

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