ArticleProtein science : a publication of the Protein Society2011
A secretory system for bacterial production of high-profile protein targets.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- A high throughput assay for measuring secreted protein based on a de novo fluorescent reporter reveals regulatory and structural insights in Salmonella type three secretion system.Protein science : a publication of the Protein Society · 2025Article
- Extracellular production of Ulp1Applied microbiology and biotechnology · 2022Article
- Mechanisms Involved in the Active Secretion of CTX-M-15 β-Lactamase by Pathogenic Escherichia coli ST131.Antimicrobial agents and chemotherapy · 2021Article
- Random and combinatorial mutagenesis for improved total production of secretory target protein in Escherichia coli.Scientific reports · 2021Article
- Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.Molecular microbiology · 2019Article
- Article
- Accelerated directed evolution of dye-decolorizing peroxidase using a bacterial extracellular protein secretion system (BENNY).Bioresources and bioprocessing · 2019Article
- Developing Gram-negative bacteria for the secretion of heterologous proteins.Microbial cell factories · 2018Review
- Novel signal peptides improve the secretion of recombinant Staphylococcus aureus Alpha toxinAMB Express · 2017Article
- A combination of HPLC and automated data analysis for monitoring the efficiency of high-pressure homogenization.Microbial cell factories · 2017Article
- Article
- Folding Optimization In Vivo Uncovers New Chaperones.Journal of molecular biology · 2015Article
- Functional production of a soluble and secreted single-chain antibody by a bacterial secretion system.PloS one · 2014Article
- Expressing the human proteome for affinity proteomics: optimising expression of soluble protein domains and in vivo biotinylation.New biotechnology · 2012Article
- Modified recombinant proteins can be exported via the Sec pathway in Escherichia coli.PloS one · 2012Article
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Authors and funding
7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli represents a robust, inexpensive expression host for the production of recombinant proteins. However, one major limitation is that certain protein classes do not express well in a biologically relevant form using standard expression approaches in the cytoplasm of E. coli. To improve the usefulness of the E. coli expression platform we have investigated combinations of promoters and selected N-terminal fusion tags for the extracellular expression of human target proteins. A comparative study was conducted on 24 target proteins fused to outer membrane protein A (OmpA), outer membrane protein F (OmpF) and osmotically inducible protein Y (OsmY). Based on the results of this initial study, we carried out an extended expression screen employing the OsmY fusion and multiple constructs of a more diverse set of human proteins. Using this high-throughput compatible system, we clearly demonstrate that secreted biomedically relevant human proteins can be efficiently retrieved and purified from the growth medium.
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