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Escherichia coli-Based Cell-Free Protein Synthesis: Protocols for a robust, flexible, and accessible platform technology
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Escherichia coli as a glycoprotein production host: recent developments and challenges
Stephen R P Jaffé1, Benjamin Strutton1, Zdenko Levarski2
1ChELSI Institute, Department of Chemical and Biological Engineering, Sir Robert Hadfield Building, Mappin Street, Sheffield S1 3JD, UK.
Current Opinion in Biotechnology
|August 27, 2014
Summary
Engineering Escherichia coli for therapeutic glycoprotein production is advancing rapidly. Researchers are improving N-glycosylation efficiency and glycan composition in E. coli, aiming for cost-effective glycoprotein manufacturing.
Area of Science:
- Biotechnology
- Molecular Biology
- Biochemistry
Background:
- Chinese Hamster Ovary (CHO) cells are the standard for producing therapeutic glycoproteins.
- Escherichia coli (E. coli) is being engineered as an alternative host system.
- The transfer of an N-glycosylation pathway from Campylobacter jejuni to E. coli in 2002 was a key development.
Purpose of the Study:
- To review recent progress in N-glycosylation of recombinant therapeutic proteins in E. coli.
- To discuss advancements in glycan composition and glycosylation efficiency.
- To highlight remaining challenges for E. coli as an industrial host.
Main Methods:
- Functional transfer of N-glycosylation pathways.
- Engineering of E. coli for enhanced glycosylation.
- Manipulation of glycan composition in E. coli.
Main Results:
- Significant advancements in engineering E. coli for N-glycosylation.
- Improvements in glycosylation efficiency and control over glycan structures.
- Demonstrated potential for E. coli in recombinant protein production.
Conclusions:
- E. coli shows promise as a host for glycoprotein production.
- Further engineering is required to achieve economically viable glycoprotein manufacturing.
- Overcoming current challenges will enable widespread industrial application.
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