Recombinant protein secretion in Escherichia coli
Abstract
The secretory production of recombinant proteins by the Gram-negative bacterium Escherichia coli has several advantages over intracellular production as inclusion bodies. In most cases, targeting protein to the periplasmic space or to the culture medium facilitates downstream processing, folding, and in vivo stability, enabling the production of soluble and biologically active proteins at a reduced process cost. This review presents several strategies that can be used for recombinant protein secretion in E. coli and discusses their advantages and limitations depending on the characteristics of the target protein to be produced.
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E. coli exploits three main pathways for protein translocation to the periplasm: the SecB-dependent, the SRP-mediated and the twin-arginine transport pathways.
“Like other Gram-negative bacteria, E. coli exploits three main pathways for protein translocation to the periplasm: the SecB-dependent, the SRP-mediated and the twin-arginine transport (TAT) translocation pathways [131,132,133].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [131]
Extracellular secretion can be successfully achieved by optimizing the induction starting point and by adding chemical agents that promote outer cell membrane permeability.
“The extracellular secretion can be successfully achieved by optimizing the induction starting point and by adding chemical agents that promote outer cell membrane permeability [131,148,173].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [131]
Cites
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Masquerading microbial pathogens: capsular polysaccharides mimic host-tissue molecules
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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
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- Authors
- Mergulhão, F. J. M., Summers, D. K., & Monteiro, G. A.
- Affiliations
- Instituto Superior Técnico (PT)
- University of Cambridge (GB)
- Corresponding author
- Mergulhão, F.J.M.
- Venue
- Biotechnology Advances
- Publisher
- Elsevier BV
- Published
- 2005-05
- Volume
- 23
- Issue
- 3
- Pages
- 177-202
- ISSN
- 0734-9750 (ISSN-L)
- OpenAlex
- W2085338944
- Cited by
- 485
- References
- 2
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 20 · 2023: 16 · 2022: 16 · 2021: 31 · 2020: 22 · 2019: 33 · 2018: 37 · 2017: 30 · 2016: 30 · 2015: 27 · 2014: 27 · 2013: 51 · 2012: 23
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biotechnology Advances (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 › Microbial Metabolic Engineering and Bioproduction
- Keywords
- recombinant protein secretion, Escherichia coli, periplasm, soluble protein production, protein folding, protein stability, inclusion bodies, downstream processing
- MeSH terms
- Bacterial Proteins, Cell Membrane, Escherichia coli, Recombinant Proteins, Protein Engineering
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