A simple high-yielding process for transient gene expression in CHO cells

Rajendra, Yashas; Kiseljak, Divor; Baldi, Lucia; Hacker, David L.; Wurm, Florian Μ.

doi:10.1016/j.jbiotec.2011.03.001

Cited by 103 publications

(96 citation statements)

References 18 publications

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“…The HEK293 cell line is easily transfectable with a variety of gene transfer reagents, and is probably the most utilized cell line for large-scale transient gene expression [28,29]. More recently, approaches using CHO cells have also been developed that provide tens to hundreds of milligrams of protein per litre [30]. In order to generate high titres of antibodies with enhanced α2,6-sialylation, we optimized the conditions for the transient coexpression of human ST6Gal-I together with IgG light and heavy chains in CHO and HEK293 cells.…”

Section: Production Of Sialylated Recombinant Antibodymentioning

confidence: 99%

Production of Highly Sialylated Monoclonal Antibodies

Raymond¹,

Robotham²,

Kelly³

et al. 2012

Glycosylation

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Section: Production Of Sialylated Recombinant Antibodymentioning

confidence: 99%

Production of Highly Sialylated Monoclonal Antibodies

Raymond¹,

Robotham²,

Kelly³

et al. 2012

Glycosylation

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“…S2) and expressed the recombinant immunocytokine either by transient gene expression (TGE) or by stable expression (SE) in stably transfected Chinese hamster ovary (CHO) cells ( Fig. 1 A and B) (18). Stably transfected polyclonal CHO cells were cultured at a higher cell density and modified medium composition.…”

Section: Resultsmentioning

confidence: 99%

Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies

Venetz¹,

Hess²,

Lin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The ability of antibodies to extravasate out of blood vessels is critical for therapeutic activity, because molecular targets for most diseases are located outside of the endothelial lining. By performing detailed biodistribution studies with a novel IL9-armed cancer-specific antibody, we identified a clear correlation between N-linked glycan structures and tumor-targeting efficiencies. Site-specific glycan analysis provided a detailed view of the glycan microheterogeneity present on the IL9 portion of the recombinant protein. Nonsialylated glycan structures have a negative impact on disease-homing activity, highlighting the importance of glycosylation control and characterization during process development.

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“…Transfections can be carried out at a high cell density to increase TGE yields as seen by 250 mg/l antibody yields from TGE in CHO cells transfected at 4  10 6 cells/ml (ref. 30). Large scale transfections require producing and purifying large amounts of plasmid DNA in E. coli.…”

Section: Host Cells and Host Cell Engineeringmentioning

confidence: 99%

Cell Culture Processes for Biopharmaceutical Manufacturing

Gadgil

2017

Current Science

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Recombinant proteins manufactured using animal cell culture processes comprise a significant fraction of biopharmaceuticals. With the expiry of patents on this class of therapeutics, there is also a significant interest in manufacture of biosimilar versions of such therapeutics. This article provides a birds-eye view of upstream process development for animal cell culture processes, with a focus on advances pertinent to the development of processes for biosimilars.

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A simple high-yielding process for transient gene expression in CHO cells

Cited by 103 publications

References 18 publications

Production of Highly Sialylated Monoclonal Antibodies

Production of Highly Sialylated Monoclonal Antibodies

Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies

Cell Culture Processes for Biopharmaceutical Manufacturing

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