ArticleAvicenna journal of medical biotechnology
Comparison of Three Escherichia coli Strains in Recombinant Production of Reteplase.
Article in Avicenna journal of medical biotechnology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
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- Refolding, Crystallization, and Crystal Structure Analysis of a Scavenger Receptor Cysteine-Rich Domain of Human Salivary Agglutinin Expressed in Escherichia coli.The protein journal · 2024Article
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
- High-Yield Expression and Purification of Scygonadin, an Antimicrobial Peptide, Using the Small Metal-Binding Protein SmbP.Microorganisms · 2024Article
- Engineering a CEACAM1 Variant with the Increased Binding Affinity to TIM-3 ReceptorIranian biomedical journal · 2023Article
- Factors involved in heterologous expression of proteins in E. coli host.Archives of microbiology · 2023Review
- Characterization ofMicrobiology spectrum · 2022Article
- Efficient and specific bioaccumulation of arsenic in the transgenic Escherichia coli expressing ArsR1 from Corynebacterium glutamicum.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- Current trends in biopharmaceuticals production in Escherichia coli.Biotechnology letters · 2022Review
- A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed inInternational journal of molecular sciences · 2022Article
- Cloning and expression analyses of aBioengineered · 2021Article
- Investigation of Supercharging as A Strategy to Enhance the Solubility and Plasminogen Cleavage Activity of Reteplase.Iranian journal of biotechnology · 2020Article
- A polyclonal antibody against a recombinantly expressed Triticum aestivum RHT-D1A protein.Journal, genetic engineering & biotechnology · 2020Article
- Evaluation of soluble expression of recombinant granulocyte macrophage stimulating factor (rGM-CSF) by three differentResearch in pharmaceutical sciences · 2020Article
- Engineered Escherichia coli strains as platforms for biological production of isoprene.FEBS open bio · 2020Article
- Anti-HER2 scFv Expression in Escherichia coli SHuffleMolecular biotechnology · 2020Article
- Reteplase: Structure, Function, and Production.Advanced biomedical research · 2019Review
- Effects of the cyclophilin-type peptidylprolyl cis-trans isomerase from Pyropia yezoensis against hydrogen peroxide-induced oxidative stress in HepG2 cells.Molecular medicine reports · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundEscherichia coli (E. coli) is the most extensively used host for the production of recombinant proteins. However, most of the eukaryotic proteins are typically obtained as insoluble, misfolded inclusion bodies that need solubilization and refolding. Reteplase as a highly disulfide-bonded recombinant protein is an example of difficult to express protein in E. coli.
methodsIn this study, a codon optimized reteplase gene was synthetically prepared and cloned under the control of an IPTG inducible T7 promoter. The vector was simultaneously transformed and expressed in three different E. coli strains. The ability of strains for expression of this recombinant pharmaceutical was compared. Also, an attempt was made to increase the soluble production of reteplase in SHuffle T7 E. coli with alterations of expression condition like temperature, inducer concentration and oxygen supply.
resultsHigh amounts of reteplase were expressed as inclusion bodies in all three strains. BL21 (DE3) showed the highest level of expression in inclusion bodies followed by Rosetta-gami (DE3) and Shuffle T7. Changes of expression conditions were insufficient for soluble expression of reteplase in SHuffle T7 as a genetically engineered host for production of disulfide bonded proteins.
conclusionThe oxidizing cytoplasm of Rosetta-gami and Shuffle T7 in addition to alterations of cultivation parameters could not result in soluble production of reteplase, although the inclusion bodies produced in these two strains might increase the rate of refolding procedure likely due to formation of folding intermediates.
Indexed as
Identifiers
26855731PMC4717461W2255047265What OpenQuestion holds
Registered trials
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