ArticleMicrobial cell factories2009
Use of folding modulators to improve heterologous protein production in Escherichia coli.
Article in Microbial cell factories, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 115 citations in OpenAlex.
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- SAS: Split antibiotic selection for identifying chaperones that improve protein solubility.Heliyon · 2024Article
- Evaluation of factors influencing expression and extraction of recombinant bacteriophage endolysins in Escherichia coli.Microbial cell factories · 2022Article
- Multimodal approaches for the improvement of the cellular folding of a recombinant iron regulatory protein in E. coli.Microbial cell factories · 2022Article
- A novel approach of recombinant laterosporulin production using the N-SH2 domain of SHP-2.BMC biotechnology · 2021Article
- The expression and characterization of recombinant cp19k barnacle cement protein from Pollicipes pollicipes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Article
- An efficient expression tag library based on self-assembling amphipathic peptides.Microbial cell factories · 2019Article
- Directed evolution to improve protein folding in vivo.Current opinion in structural biology · 2018Review
- One-step purification and immobilization of extracellularly expressed sortase A by magnetic particles to develop a robust and recyclable biocatalyst.Scientific reports · 2017Article
- Protein folding in the cell envelope of Escherichia coli.Nature microbiology · 2016Review
- 3'-UTR engineering to improve soluble expression and fine-tuning of activity of cascade enzymes in Escherichia coli.Scientific reports · 2016Article
- Engineering of Baeyer-Villiger monooxygenase-based Escherichia coli biocatalyst for large scale biotransformation of ricinoleic acid into (Z)-11-(heptanoyloxy)undec-9-enoic acid.Scientific reports · 2016Article
- Article
- Folding Optimization In Vivo Uncovers New Chaperones.Journal of molecular biology · 2015Article
- Antigen production using heterologous expression of dengue virus-2 non-structural protein 1 (NS1) in Nicotiana tabacum (Havana) for immunodiagnostic purposes.Plant cell reports · 2015Article
- Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system.Frontiers in microbiology · 2014Review
- Improved detection of domoic acid using covalently immobilised antibody fragments.Marine drugs · 2013Article
- Production of the catalytic core of human peptidylglycine α-hydroxylating monooxygenase (hPHMcc) in Escherichia coli.Protein expression and purification · 2012Article
- Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements.Journal of industrial microbiology & biotechnology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the fundamental importance of E. coli in the manufacture of a wide range of biotechnological and biomedical products, extensive process and/or target optimisation is routinely required in order to achieve functional yields in excess of low mg/l levels. Molecular chaperones and folding catalysts appear to present a panacea for problems of heterologous protein folding in the organism, due largely to their broad substrate range compared with, e.g., protein-specific mutagenesis approaches. Painstaking investigation of chaperone overproduction has, however, met with mixed - and largely unpredictable - results to date. The past 5 years have nevertheless seen an explosion in interest in exploiting the native folding modulators of E. coli, and particularly cocktails thereof, driven largely by the availability of plasmid systems that facilitate simultaneous, non-rational screening of multiple chaperones during recombinant protein expression. As interest in using E. coli to produce recombinant membrane proteins and even glycoproteins grows, approaches to reduce aggregation, delay host cell lysis and optimise expression of difficult-to-express recombinant proteins will become even more critical over the coming years. In this review, we critically evaluate the performance of molecular chaperones and folding catalysts native to E. coli in improving functional production of heterologous proteins in the bacterium and we discuss how they might best be exploited to provide increased amounts of correctly-folded, active protein for biochemical and biophysical studies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.