ArticleScientific reports2023
Efficient production of recombinant proteins in suspension CHO cells culture using the Tol2 transposon system coupled with cycloheximide resistance selection.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- Production of multi-subunit proteins in CHO cells by transposase-mediated integration of subunit-splitting vectors.Scientific reports · 2025Article
- Feedback-responsive cell factories for dynamic modulation of the unfolded protein response.Nature communications · 2025Article
- Establishment of an indirect ELISA method for detecting bovine coronavirus antibodies based on N protein.Frontiers in veterinary science · 2025Article
- Promoting the production of challenging proteins via induced expression in CHO cells and modified cell-free lysates harboring T7 RNA polymerase and mutant eIF2α.Synthetic and systems biotechnology · 2024Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
DNA recombination techniques in mammalian cells has been applied to the production of therapeutic proteins for several decades. To be used for commercial production, established cell lines should stably express target proteins with high productivity and acceptable quality for human use. In the conventional transfection method, the screening process is laborious and time-consuming since superior cell lines had to be selected from an enormous number of transfected cell pools and clonal cell lines with a wide variety of transgene insertion locations. In this study, we demonstrated that the combination of a Tol2 transposon system and cell selection by cycloheximide resistance is an efficient method to express therapeutic proteins, such as human antibody in suspension culture of Chinese hamster ovary cells. The resulting stable cell lines showed constant productivity and cell growth over a long enough cultivation periods for recombinant protein production. We anticipate that this approach will prove widely applicable to protein production in research and development of pharmaceutical products.
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