Construction of Expression Vectors for Efficient Production of Recombinant Proteins in E. coli for the Development of Therapeutic Drugs

Jia, B. and Jeon, C.O., High-throughput recombinant protein expression in Escherichia coli: Current status and future perspectives, Open Biol., 2016, vol. 6, no. 8, p. 160196.

Article  PubMed  PubMed Central  Google Scholar 

Ortega, C., Oppezzo, P., and Correa, A., Overcoming the solubility problem in E. coli: Available approaches for recombinant protein production, in Methods Mol. Biol., 2022, vol. 2406, pp. 35–64.

Article  CAS  PubMed  Google Scholar 

Rosano, G.L. and Ceccarelli, E.A., Rare codon content affects the solubility of recombinant proteins in a codon bias-adjusted Escherichia coli strain, Microb. Cell Fact., 2009, vol. 8, p. 41.

Article  PubMed  PubMed Central  Google Scholar 

Kamionka, M., Engineering of therapeutic proteins production in Escherichia coli, Curr. Pharm. Biotechnol., 2011, vol. 12, no. 2, pp. 268–274.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Pacheco, B., Crombet, L., Loppnau, P., et al., A screening strategy for heterologous protein expression in Escherichia coli with the highest return of investment, Protein Expression Purif., 2012, vol. 81, no. 1, pp. 33–41.

Article  CAS  Google Scholar 

Samuelson, J.C., Recent developments in difficult pro-tein expression: A guide to E. coli strains, promoters, and relevant host mutations, in Heterologous Gene Expression in E. coli: Methods and Protocols, Evans, T.C., Jr. and Xu, M.-Q., Eds., Methods in Molecular Biology, vol. 705, New York: Humana, 2011, pp. 195–209.

Yang, Z., Zhang, L., Zhang, Y. et al., Highly efficient production of soluble proteins from insoluble inclusion bodies by a two-step-denaturing and refolding method, PLoS One, 2011, vol. 6, no. 7, p. e22981.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Nishihara, K., Kanemori, M., Kitagawa, M., et al., Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli, Appl. Environ. Microbiol., 1998, vol. 64, pp. 1694–1699.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Nishihara, K., Kanemori, M., Yanagi, H., et al., Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli, Appl. Environ. Microbiol., 2000, vol. 66, pp. 884–889.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Rosano, G.L. and Ceccarelli, E.A., Recombinant protein expression in Escherichia coli: Advances and challenges, Front. Microbiol., 2014, vol. 5, p. 172.

Article  PubMed  PubMed Central  Google Scholar 

Young, C.L., Britton, Z.T., and Robinson, A.S., Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications, Biotechnol. J., 2012, vol. 7, no. 5, pp. 620–634.

Article  CAS  PubMed  Google Scholar 

Waugh, D.S., Making the most of affinity tags, Trends Biotechnol., 2005, vol. 23, no. 6, pp. 316–320.

Article  CAS  PubMed  Google Scholar 

Nozach, H., Fruchart-Gaillard, C., Fenaille, F., et al., High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli, Microb. Cell Fact., 2013, vol. 12, no. 1, p. 37.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Costa, S., Almeida, A., Castro, A., et al., Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: The novel Fh8 system, Front. Microbiol., 2014, vol. 5, p. 63.

Article  PubMed  PubMed Central  Google Scholar 

Loughran, S.T. and Walls, D., Tagging recombinant proteins to enhance solubility and aid purification, in Protein Chromatography: Methods and Protocols, Walls, D. and Loughran, S.T., Eds., Methods in Molecular Biology, vol. 1485, New York: Humana, 2017, pp. 131–156.

Studier, F.W. and Moffatt, B.A., Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes, J. Mol. Biol., 1986, vol. 189, no. 1, pp. 113–130.

Article  CAS  PubMed  Google Scholar 

Stano, N.M. and Patel, S.S., T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation, J. Biol. Chem., 2004, vol. 279, no. 16, pp. 16136–16143.

Article  CAS  PubMed  Google Scholar 

Van Den Berg, S., Löfdahl, P.-A., Härd, T., et al., Improved solubility of TEV protease by directed evolution, J. Biotechnol., 2006, vol. 121, no. 3, pp. 291–298.

Article  CAS  PubMed  Google Scholar 

Schäfer, F., Seip, N., Maertens, B., et al., Purification of GST-tagged proteins, Methods Enzymol., 2015, vol. 559, pp. 127–139.

Bonhoure, A., Demenge, A., Kostmann, C., et al., One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: Application to aggregation-prone HPV E6 proteins, Microb. Cell Fact., 2018, vol. 17, no. 1, p. 191.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Do, B.H., Park, S., Kwon, G.G., et al., Soluble expression and purification of bioactive interleukin 33 in E. coli, Biotechnol. Bioprocess Eng., 2017, vol. 22, no. 3, pp. 256–264.

Article  CAS  Google Scholar 

Kim, Y.V., Gasparian, M.E., Bocharov, E.V., et al., New strategy for high-level expression and purification of biologically active monomeric TGF-β1/C77S in Escherichia coli, Mol. Biotechnol., 2015, vol. 57, no. 2, pp. 160–171.

Article  CAS  PubMed  Google Scholar 

Rasooli, F. and Hashemi, A., Efficient expression of EpEX in the cytoplasm of Escherichia coli using thioredoxin fusion protein, Res. Pharm. Sci., 2019, vol. 14, no. 6, p. 554.

Article  PubMed  PubMed Central  Google Scholar 

Zakharova, M.V., Zagoskin, A.A., Ivanov, R.A., and Nagornykh, M.O., Production of a recombinant ribonuclease inhibitor in E. coli for use in in vitro mRNA synthesis, Vestn. Ross. Gos. Med. Univ., 2023, vol. 6, pp. 36–44.

Google Scholar 

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