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Optimisation of signal peptide for recombinant protein secretion in bacterial hosts

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Abstract

Escherichia coli—the powerhouse for recombinant protein production—is rapidly gaining status as a reliable and efficient host for secretory expression. An improved understanding of protein translocation processes and its mechanisms has inspired and accelerated the development of new tools and applications in this field and, in particular, a more efficient secretion signal. Several important characteristics and requirements are summarised for the design of a more efficient signal peptide for the production of recombinant proteins in E. coli. General approaches and strategies to optimise the signal peptide, including the selection and modification of the signal peptide components, are included. Several challenges in the secretory production of recombinant proteins are discussed, and research approaches designed to meet these challenges are proposed.

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Acknowledgements

We would like to thank Noor Faizah Ismail for the critical reading of the manuscript. Support from Abdul Munir Abdul Murad, Amir Rabu and Farah Diba Abu Bakar of Universiti Kebangsaan Malaysia and Raha Abdul Rahim of Universiti Putra Malaysia is greatly appreciated. This work was supported by the Genomics and Molecular Biology Initiatives Programme of the Malaysia Genome Institute, Ministry of Science, Technology and Innovation Malaysia (Project No. 07-05-MGI-GMB011) and the Exploration Research Grant Scheme (R.J130000.7835.4L046), Universiti Teknologi Malaysia. Kheng Oon Low is a researcher of Universiti Teknologi Malaysia under the Post-Doctoral Fellowship Scheme.

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Correspondence to Rosli Md. Illias.

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Low, K.O., Muhammad Mahadi, N. & Md. Illias, R. Optimisation of signal peptide for recombinant protein secretion in bacterial hosts. Appl Microbiol Biotechnol 97, 3811–3826 (2013). https://doi.org/10.1007/s00253-013-4831-z

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  • DOI: https://doi.org/10.1007/s00253-013-4831-z

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