Effect of DnaK/DnaJ/GrpE and DsbC Chaperons on Periplasmic Expression of Fab Antibody by E. coli SEC Pathway
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Coexpression of DnaK/DnaJ/GrpE results in a 2.5-fold increase in the periplasmic expression level of an anti-TNF-α Fab in shake flasks using LB medium and BL21(DE3) strains.
“For instance, Dariushnejad and coworkers have reported that the coexpression of DnaK/DnaJ/GrpE (DnaKJE) results in a 2.5-fold increase in the periplasmic expression level of an anti-TNF-α Fab in shake flasks, using LB medium and BL21(DE3) strains [99,100].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [99]
DsbC overexpression in the cytoplasm exerts a positive effect on the solubility of cytoplasmic proteins, not on recombinant proteins that are targeted to the periplasmic space.
“Taken together these data suggest that DsbC overexpression in the cytoplasm exerts a positive effect on the solubility of cytoplasmic proteins [113] not on the recombinant proteins that are targeted to the periplasmic space [99].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [99]
Fab fragments bearing the OmpA signal peptide were efficiently produced as soluble periplasmic products by coexpression with DnaK/DnaJ/GrpE in shake flasks using LB medium and inducing with 0.1 mM IPTG at 25 °C for 8 h.
“Additionally, Fab fragments bearing the OmpA signal peptide were efficiently produced as soluble periplasmic products by coexpression with DnaK/DnaJ/GrpE in shake flasks using the LB medium and inducing with 0.1 mM IPTG at 25 °C for 8 h [99].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [99]
Cites
Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
Sørensen, H. P., & Mortensen, K. K. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-1 · Cited by 841 · see citing works
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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
“While the preparation of whole antibody molecules requires eukaryotic expression systems, antibody fragments like Fabs, scFvs and other similar surrogates that lack the glycosylation, can be conveniently prepared in E. coli backgrounds.”
BackgroundMethodInfluential
- Authors
- Dariushnejad, H., Farajnia, S., Zarghami, N., Aria, M., & Tanomand, A.
- Affiliations
- Tabriz University of Medical Sciences (IR)
- Maragheh University of Medical Sciences (IR)
- Corresponding author
- Farajnia, Safar
- Venue
- International Journal of Peptide Research and Therapeutics
- Published
- 2017-11-27
- Volume
- 25
- Issue
- 1
- Pages
- 67-74
- ISSN
- 1573-3149 (ISSN-L)
- 1573-3904
- OpenAlex
- W2768175435
- Cited by
- 19
- References
- 1
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 1 · 2023: 2 · 2022: 3 · 2021: 6 · 2020: 1 · 2019: 1
- FWCI
- 0.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- International Journal of Peptide Research and Therapeutics (publishedVersion)
- Funders
- Drug Applied Research Center, Tabriz University of Medical Sciences (94/54)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Keywords
- antibody Fab fragment, periplasmic expression, disulfide bond formation, anti-TNF-alpha antibody, inclusion body formation, protein solubility, co-expression, recombinant expression in Escherichia coli
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