ArticleThe protein journal2014
Improved expression of recombinant human factor IX by co-expression of GGCX, VKOR and furin.
Article in The protein journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Cell Engineering for Increasing Production of Recombinant Proteins in Mammalian Cells.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- PBPK modeling of recombinant factor IX Fc fusion protein (rFIXFc) and rFIX to characterize the binding to type 4 collagen in the extravascular space.CPT: pharmacometrics & systems pharmacology · 2024Article
- Structural, functional, and immunogenicity implications of F9 gene recoding.Blood advances · 2022Article
- Article
- Monoclonal antibodies expression improvement in CHO cells by PiggyBac transposition regarding vectors ratios and design.PloS one · 2017Article
- Posttranslational Modifications and the Immunogenicity of Biotherapeutics.Journal of immunology research · 2016Review
- Mini-review on "A novel one-step purification of mouse factor IX".Journal of rare diseases research & treatment · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recombinant human FIX concentrates (rhFIX) are essential in the treatment and prevention of bleeding in the bleeding disorder haemophilia B. However, due to the complex nature of FIX production yields are low which leads to high treatment costs. Here we report the production of rhFIX with substantially higher yield by co-expressing human FIX with GGCX (γ-glutamyl carboxylase), VKOR (vitamin K epoxide reductase) and furin (paired basic amino acid cleaving enzyme) in Chinese hamster ovary (CHO) cells. Our results show that controlled co-expression of GGCX with FIX is critical to obtain high rhFIX titre, and, that co-expression of VKOR further increased the yield of active rhFIX. Furin co-expression improved processing of the leader peptide of rhFIX but had a minor effect on yield of active rhFIX. The optimal expression level of GGCX was surprisingly low and required unusual engineering of expression vector elements. For VKOR and furin the control of expression was less critical and could be achieved by standard vector element. Using our expression vectors an rhFIX-producing clone with an expression level of up to 30 mg/L of active rhFIX was obtained. In addition an efficient single step purification method was developed to obtain pure and active rhFIX with up to 94% yield.
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Registered trials
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