Development of the system ensuring a high-level expression of hepatitis C virus nonstructural NS5B and NS5A proteins

Ivanov, Alexander V.; Коровина, А. Н.; Tunitskaya, V. L.; Kostyuk, D. A.; Rechinsky, Vladimir O.; Kukhanova, Marina K.; Kochetkov, S. N.

doi:10.1016/j.pep.2006.02.011

Cited by 52 publications

(40 citation statements)

References 34 publications

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“…This strain is especially more eYcient at expressing proteins that are diYcult to express in E. coli BL21 (DE3). The use of the pRARE plasmid is a practical method to improve the yield of heterologous proteins in E. coli and has been demonstrated in several studies [30,33,37].…”

Section: Protein Translationmentioning

confidence: 99%

Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements

Huang

Lin

Yang

2012

Journal of Industrial Microbiology and Biotechnology

366

248

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Nearly 30% of currently approved recombinant therapeutic proteins are produced in Escherichia coli. Due to its well-characterized genetics, rapid growth and high-yield production, E. coli has been a preferred choice and a workhorse for expression of non-glycosylated proteins in the biotech industry. There is a wealth of knowledge and comprehensive tools for E. coli systems, such as expression vectors, production strains, protein folding and fermentation technologies, that are well tailored for industrial applications. Advancement of the systems continues to meet the current industry needs, which are best illustrated by the recent drug approval of E. coli produced antibody fragments and Fc-fusion proteins by the FDA. Even more, recent progress in expression of complex proteins such as full-length aglycosylated antibodies, novel strain engineering, bacterial N-glycosylation and cell-free systems further suggests that complex proteins and humanized glycoproteins may be produced in E. coli in large quantities. This review summarizes the current technology used for commercial production of recombinant therapeutics in E. coli and recent advances that can potentially expand the use of this system toward more sophisticated protein therapeutics.

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Section: Protein Translationmentioning

confidence: 99%

Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements

Huang

Lin

Yang

2012

Journal of Industrial Microbiology and Biotechnology

366

248

View full text Add to dashboard Cite

show abstract

“…Poor intensity of recombinant protein biosynthesis in the system with T7 promotor could be caused by disagreement between the rates of transcription and translation because of bacterial promotor replacement with T7 promotor. The resultant transcript not protected by ribosomes became a target for nucleases [6].…”

Section: Resultsmentioning

confidence: 99%

Expression of a Recombinant Extracellular Fragment of Human Vascular Endothelial Growth Factor Receptor VEGFR1 in E. coli

et al. 2011

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Human vascular endothelium growth factor receptor VEGFR1 is a type III fms-like tyrosine kinase with weakly pronounced tyrosine kinase function. The second and third IgG-like domains of the extracellular part of VEGFR1 act as "traps" for VEGF and are prospective candidates for antiangiogenic therapy of VEGF-dependent tumors. cDNA encoding extracellular Ig-like domains 2, 3, 4 of VEGFR1 was cloned in expressing vectors pET28a, pET32a, and pQE60. The recombinant protein was expressed in E. coli cells and purified by metal affinity chromatography. An expressing construction and a superproducer strain were created, allowing the production of high amounts of recombinant VEGFR1 extracellular fragment, needed for experimental in vivo antiangiogenic therapy.

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“…Two additional amino acid residues (Met, Asn) were located on the protein N terminus as against the native protein (RB01 HCV isolate). The enzyme was isolated and purified as we described previously [11].…”

Section: Methodsmentioning

confidence: 99%

Non-hydrolysable analogues of inorganic pyrophosphate as inhibitors of hepatitis C virus RNA-dependent RNA-polymerase

et al. 2012

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Inorganic pyrophosphate (PP i ) is the product of the polymerization reaction catalyzed by DNA and RNA polymerases. A number of novel non hydrolsable PP i analogues was synthesized; some of them inhibited the polymerization reaction catalyzed by hepatitis C virus RNA dependent RNA polymerase (NS5B). A new pharmacophore based on a non hydrolysable methylenediphosphonate backbone has been developed. The structure activity relationship analysis of 12 bisphosphonates is presented and the structural features crucial for NS5B polymerase activity inhibition are stated.

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Development of the system ensuring a high-level expression of hepatitis C virus nonstructural NS5B and NS5A proteins

Cited by 52 publications

References 34 publications

Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements

Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements

Expression of a Recombinant Extracellular Fragment of Human Vascular Endothelial Growth Factor Receptor VEGFR1 in E. coli

Non-hydrolysable analogues of inorganic pyrophosphate as inhibitors of hepatitis C virus RNA-dependent RNA-polymerase

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