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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
21.7K
Multiplex secretome engineering enhances recombinant protein production and purity
Stefan Kol1, Daniel Ley2, Tune Wulff2
1The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Building 220, Kemitorvet, 2800, Kgs. Lyngby, Denmark. stef.kol@gmail.com.
Nature Communications
|April 22, 2020
Summary
We engineered Chinese hamster ovary (CHO) cells to reduce host cell proteins (HCPs), a common impurity in biotherapeutics. This strategy significantly lowered HCP levels, improving protein production and purification for more affordable, high-quality biopharmaceuticals.
Area of Science:
- Biotechnology
- Cell Biology
- Protein Engineering
Background:
- Host cell proteins (HCPs) are critical impurities in biotherapeutic production, impacting product quality and safety.
- Reducing HCPs is essential for efficient purification and to meet regulatory standards.
Purpose of the Study:
- To develop a "cleaner" Chinese hamster ovary (CHO) cell line with significantly reduced HCP levels.
- To assess the impact of HCP reduction on cell growth, protein productivity, and purification efficiency.
Main Methods:
- Utilized gene disruption techniques to create multiple knockout CHO cell clones.
- Analyzed HCP content in engineered cell lines using quantitative methods.
- Evaluated cell growth characteristics and productivity of modified clones.
Main Results:
- Engineered CHO cell lines demonstrated a 40%-70% reduction in total HCP content.
- Specific knockout clones exhibited enhanced productivity and improved growth.
- Reduced HCP levels facilitated more efficient purification of a monoclonal antibody.
Conclusions:
- Large-scale HCP deletion in CHO cells is a viable strategy to improve biopharmaceutical quality and affordability.
- This approach offers a promising avenue for enhancing protein titer and purity in biomanufacturing.
