Manufacturing of recombinant therapeutic proteins in microbial systems

@article{Graumann2006ManufacturingOR,
  title={Manufacturing of recombinant therapeutic proteins in microbial systems},
  author={Klaus Graumann and Andreas Premstaller},
  journal={Biotechnology Journal},
  year={2006},
  volume={1}
}
Recombinant therapeutic proteins have gained enormous importance for clinical applications. The first recombinant products have been produced in E. coli more than 20 years ago. Although with the advent of antibody‐based therapeutics mammalian expression systems have experienced a major boost, microbial expression systems continue to be widely used in industry. Their intrinsic advantages, such as rapid growth, high yields and ease of manipulation, make them the premier choice for expression of… Expand

Topics from this paper

Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements
TLDR
The current technology used for commercial production of recombinant therapeutics in E. coli is summarized and recent advances that can potentially expand the use of this system toward more sophisticated protein therapeutics are summarized. Expand
Cellular engineering for therapeutic protein production: product quality, host modification, and process improvement
TLDR
Recent developments for improving protein production in E. coli, S. cerevisiae, and CHO systems are described and compared to previous knowledge in the field to serve as the framework for future discoveries. Expand
Pharmaceutical protein production by yeast: towards production of human blood proteins by microbial fermentation.
TLDR
This review summarizes the main achievements and the current situation in the field of recombinant therapeutics using yeast Saccharomyces cerevisiae as a model platform, and discusses the future potential of this platform for production of blood proteins and substitutes. Expand
Therapeutic glycoprotein production in mammalian cells.
TLDR
The advance of "omics" technologies has recently given rise to new possibilities in improving these expression platforms and will significantly help developing new strategies, in particular for CHO (Chinese Hamster Ovary) cells. Expand
Environmental and recombinant microorganisms for biopharmaceuticals production
TLDR
The current application of microbes as production platforms for recombinant proteins and its genetic engineering for the use as biopharmaceuticals is presented. Expand
Process Development of Protein Therapeutics
TLDR
This chapter will discuss some of the tools, methods, and approaches used to produce, purify, formulate, and analyze the drugs of modern biotechnology. Expand
Production of Recombinant Proteins in Bacteria: The Inclusion Bodies Formation and their Use in Biomedicine
TLDR
It is revealed that friendlier bacterial cultivation leads to production of non-classical IBs (ncIBs), which are composed of properly folded and biologically active proteins, which can be used either for protein isolation (production) or as active nanoparticles. Expand
Production and Purification of Recombinant Proteins from Escherichia coli
TLDR
The bioproducts obtained after fermentation and purification processes may fulfill the requirements for the development of various diagnostics, therapeutics, or prophylactic agents against different kinds of diseases. Expand
Active Protein Aggregates Produced in Escherichia coli
TLDR
Since recombinant proteins are widely used in industry and in research, the need for their low-cost production is increasing, and interest in understanding the mechanisms of their formation as well as their properties is increasing. Expand
Quality and cost assessment of a recombinant antibody fragment produced from mammalian, yeast and prokaryotic host cells: A case study prior to pharmaceutical development.
TLDR
Results show higher titer production when using E. coli but associated with high heterogeneity of the protein content recovered in the supernatant, while Fab secreted from CHO was the most homogeneous despite a much longer culture time and slightly higher estimated cost of goods. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 282 REFERENCES
Recombinant antimicrobial peptides efficiently produced using novel cloning and purification processes
TLDR
This work has developed cost‐effective methods for recombinant production by expressing fusion proteins comprised of multiple copies of the peptides that are efficacious against antibiotic‐resistant and clinically relevant pathogens. Expand
RETRACTED ARTICLE: Strategies for efficient production of heterologous proteins in Escherichia coli
TLDR
In recent years, the number of recombinant proteins used for therapeutic applications has increased dramatically, and production of these proteins has a remarkable demand in the market, with major challenges is obtaining the high yield of protein at low cost. Expand
Antibodies and Genetically Engineered Related Molecules: Production and Purification
TLDR
This review aims to highlight the current trends in the design and construction of genetically engineered antibodies and related molecules, the recombinant systems used for their production, and the development of novel affinity‐based strategies for antibody recovery and purification. Expand
Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
TLDR
Recent advances in the glycoengineering of yeasts and the expression of therapeutic glycoproteins in humanized yeasts have shown significant promise, and are challenging the current dominance of therapeutic protein production based on mammalian cell culture. Expand
Recombinant protein expression for therapeutic applications.
TLDR
In recent years, the number of recombinant proteins used for therapeutic applications has increased dramatically, and these demands have driven the development of a variety of improvements in protein expression technology, particularly involving mammalian and microbial culture systems. Expand
Advances in Escherichia coli production of therapeutic proteins.
  • J. Swartz
  • Biology, Medicine
  • Current opinion in biotechnology
  • 2001
TLDR
This work has shown that recent progress in oxidative cytoplasmic folding and cell-free protein synthesis offers attractive alternatives to standard expression methods in Escherichia coli. Expand
Preparative expression of secreted proteins in bacteria: status report and future prospects.
TLDR
The expression of heterologous secreted proteins in Escherichia coli is widely employed for laboratory and preparative purposes and protein design and directed evolution approaches are beginning to be exploited for engineering of the cellular protein folding machinery to achieve further improvements in protein expression. Expand
Bacillus subtilis as a tool for vaccine development: from antigen factories to delivery vectors.
TLDR
The status of B. subtilis-based vaccine research, either as protein factories or delivery vectors, and some alternatives for a better use of genetically modified strains are presented. Expand
Filamentous fungi as cell factories for heterologous protein production.
TLDR
This review of current practice reveals that molecular tools have enabled several new developments but it has been process development that has driven the final breakthrough to achieving commercially relevant quantities of protein. Expand
Review applications of capillary electrophoresis to the analysis of biotechnology‐derived therapeutic proteins
TLDR
Applications of mass spectrometry as an ancillary technique, used in conjunction with CE, are covered briefly and the use of antibodies as therapeutic proteins is growing and currently antibodies are the largest class of proteins produced by biotechnology. Expand
...
1
2
3
4
5
...