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Heterologous biopharmaceutical protein expression in Streptomyces
C Binnie1, J D Cossar, D I Stewart
1Cangene Corporation, Mississauga, Ontario, Canada. cbinnie@compuserve.com
Trends in Biotechnology
|August 1, 1997
Summary
Streptomyces lividans efficiently secretes human proteins for therapeutic use. This well-characterized bacterium offers a commercially viable system for recombinant protein production due to its high-biomass fermentation and low protease activity.
Area of Science:
- Biotechnology
- Microbiology
- Biochemistry
Background:
- Commercial production of therapeutic human proteins using recombinant microorganisms is established.
- Bacterial secretion systems enable extracellular release of folded, bioactive proteins.
- Streptomycetes are nonpathogenic filamentous bacteria known for high-volume protein secretion.
Purpose of the Study:
- To highlight the potential of Streptomyces lividans for commercial-scale human protein production.
- To identify key factors enabling efficient recombinant protein secretion in S. lividans.
Main Methods:
- Utilizing established plasmid-based expression systems in Streptomyces lividans.
- Implementing high-biomass fermentation processes.
- Leveraging the inherent low endogenous protease activity of S. lividans.
Main Results:
- Streptomyces lividans demonstrates the capacity for commercially viable secretion of human proteins.
- The bacterium's natural protein secretion ability is key to its utility.
- Established expression systems and fermentation processes support large-scale production.
Conclusions:
- Streptomyces lividans is a suitable host for the commercial production of recombinant human proteins.
- The combination of efficient secretion, established systems, and low protease activity makes S. lividans advantageous.
- This system supports the development of therapeutic proteins.