Recent contributions in the field of the recombinant expression of disulfide bonded protein in bacteria

Ario De Marco

doi:10.1186/1475-2859-11-129

Abstract

The production of heterologous disulfide bonded proteins in bacteria remains a biotechnological challenge. A rapid literature survey results in the identification of some interesting proposals, such as the option of producing functional proteins in the cytoplasm in the presence of sulfhydryl oxidases and isomerases. Furthermore, an ever-increasing number of applications refers to recombinant proteins displayed at the bacterial surface. Time will tell whether these developments will lead to universally accepted laboratory protocols.

Highlights

The production of heterologous disulfide bonded proteins in bacteria remains a biotechnological challenge
A) Be fit: optimize the conditions Trivial as it may sound, optimized cell factories are more efficient than unsuitable bacteria, but what features make them perform better? For instance, it is known that recombinant expression in bacteria can be substantially improved by the co-expression of molecular foldases and the addition of osmolytes, albeit the outcome is extremely protein-dependent [1]
B) In the periplasm, but better than ever Recombinant disulfide bonded proteins have been preferentially produced in the bacterial periplasmic space because of its favourable redox conditions

Summary

Conclusions

Recombinant protein production is still far from being a mature discipline and the innovative contributions briefly listed in this compendium show clearly that the platform constantly moves forward. Some tactics, such as secretion strategies and combinatorial approaches, seem to gain attention whereas other methods, such as refolding from inclusion bodies [32], have not significantly developed lately. 5. Makino T, Skretas G, Georgiou G: Strain engineering for improved expression of recombinant proteins in bacteria. 6. Ghosh C, Gupta R, Mukherjee KJ: An inverse metabolic engineering approach for the design of an improved host platform for overexpression of recombinant proteins in Escherichia coli.

Menzella HG

24. Berkmen M