ArticlePloS one2013
Recombinant production of human interleukin 6 in Escherichia coli.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- Overexpression of human interleukin 6 in NaCl inducible bacterial system and its characterization.Applied biochemistry and biotechnology · 2026Article
- Overexpression of human interleukin 6 in NaCl inducible bacterial system and its characterization.Applied biochemistry and biotechnology · 2026Article
- Overexpression of human interleukin 6 in NaCl inducible bacterial system and its characterization.Applied biochemistry and biotechnology · 2026Article
- The Effects of Lactose Induction on a Plasmid-FreeBioengineering (Basel, Switzerland) · 2020Article
- Development of nsP2 protease based cell free high throughput screening assay for evaluation of inhibitors against emerging Chikungunya virus.Scientific reports · 2018Article
- Efficient soluble expression of disulfide bonded proteins in the cytoplasm of Escherichia coli in fed-batch fermentations on chemically defined minimal media.Microbial cell factories · 2017Article
- Evaluation of antibody response against recombinant domain III proteins of dengue virus type 1 and 2.AIMS microbiology · 2017Article
- Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coli.BMC biotechnology · 2016Article
- Systems Metabolic Engineering of Escherichia coli.EcoSal Plus · 2016Review
- Stable Expression of Basic Fibroblast Growth Factor in Chloroplasts of Tobacco.International journal of molecular sciences · 2015Article
- Recombinant glucagon: a differential biological activity.AMB Express · 2015Article
- Cloning, soluble expression, and purification of the RNA polymerase II subunit RPB5 from Saccharomyces cerevisiae.Bioengineered · 2015Article
- Comparative evaluation of recombinant protein production in different biofactories: the green perspective.BioMed research international · 2014Review
- To fuse or not to fuse: what is your purpose?Protein science : a publication of the Protein Society · 2013Review
- High-level transient expression of ER-targeted human interleukin 6 in Nicotiana benthamiana.PloS one · 2012Article
- Comparison of Three Escherichia coli Strains in Recombinant Production of Reteplase.Avicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we compared basic expression approaches for the efficient expression of bioactive recombinant human interleukin-6 (IL6), as an example for a difficult-to-express protein. We tested these approaches in a laboratory scale in order to pioneer the commercial production of this protein in Escherichia coli (E. coli). Among the various strategies, which were tested under Research and Development (R&D) conditions, aggregation-prone IL6 was solubilized most effectively by co-expressing cytoplasmic chaperones. Expression of a Glutathion-S-Transferase (GST) fusion protein was not efficient to increase IL6 solubility. Alteration of the cultivation temperature significantly increased the solubility in both cases, whereas reduced concentrations of IPTG to induce expression of the T7lac-promotor only had a positive effect on chaperone-assisted expression. The biological activity was comparable to that of commercial IL6. Targeting the expressed protein to an oxidizing environment was not effective in the generation of soluble IL6. Taken together, the presence of chaperones and a lowered cultivation temperature seem effective to isolate large quantities of soluble IL6. This approach led to in vivo soluble, functional protein fractions and reduces purification and refolding requirements caused by downstream purification procedures. The final yield of soluble recombinant protein averaged approximately 2.6 mg IL6/liter of cell culture. These findings might be beneficial for the development of the large-scale production of IL6 under the conditions of current good manufacturing practice (cGMP).
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