Optimisation of signal peptide for recombinant protein secretion in bacterial hosts
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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The choice of signal peptide sequence and co-expression with chaperones can affect secretion and folding.
“Additionally, the choice of the signal peptide sequence [146,147,148,149] and the co-expression with chaperons can affect the secretion and folding (see Figure 1).”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [146]
Cites
SignalP 4.0: discriminating signal peptides from transmembrane regions
Petersen, T. N., Brunak, S., von Heijne, G., & Nielsen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1701 · Cited by 8,847 · see citing works
Coupling between codon usage, translation and protein export in <i>Escherichia coli</i>
Zalucki, Y. M., Beacham, I. R., & Jennings, M. P. (2011) · Biotechnology Journal · doi:10.1002/biot.201000334 · Cited by 21 · see citing works
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Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
Karyolaimos, A., Ampah-Korsah, H., Hillenaar, T., Mestre Borras, A., Dolata, K. M., Sievers, S., Riedel, K., Daniels, R., & de Gier, J.-W. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01511 · Cited by 66 · see citing works
Bao, R.-M., Yang, H.-M., Yu, C.-M., Zhang, W.-F., & Tang, J.-B. (2016) · Protein Expression and Purification · doi:10.1016/j.pep.2016.05.007 · Cited by 31 · see citing works
- Authors
- Low, K. O., Muhammad Mahadi, N., & Md. Illias, R.
- Affiliations
- University of Technology Malaysia (MY)
- ORCID
- Low, Kheng Oon
- Venue
- Applied Microbiology and Biotechnology
- Published
- 2013-03-26
- Volume
- 97
- Issue
- 9
- Pages
- 3811-3826
- ISSN
- 0175-7598 (ISSN-L)
- 1432-0614
- OpenAlex
- W2046083957
- Cited by
- 130
- References
- 2
- Citations by year
- 2026: 5 · 2025: 14 · 2024: 11 · 2023: 9 · 2022: 14 · 2021: 8 · 2020: 10 · 2019: 15 · 2018: 14 · 2017: 8 · 2016: 10 · 2015: 7 · 2014: 3 · 2013: 2
- FWCI
- 0.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Applied Microbiology and Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- signal peptide, recombinant protein secretion, Escherichia coli, protein translocation, bacterial secretion systems
- MeSH terms
- Bacterial Proteins, Escherichia coli, Mutation, Recombinant Proteins, Protein Transport
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