Abstract
Appropriate treatment of Hemophilia B is vital for patients’ quality of life. Historically, the treatment used was the administration of coagulation Factor IX derived from human plasma. Advancements in recombinant technologies allowed Factor IX to be produced recombinantly. Successful recombinant production has triggered a gradual shift from the plasma derived origins of Factor IX, as it provides extended half-life and expanded production capacity. However, the complex post-translational modifications of Factor IX have made recombinant production at scale difficult. Considerable research has therefore been invested into understanding and optimizing the recombinant production of Factor IX. Here, we review the evolution of recombinant Factor IX production, focusing on recent developments in bioprocessing and cell engineering to control its post-translational modifications in its expression from Chinese Hamster Ovary (CHO) cells.
Acknowledgements
The authors would like to thank the National Biologics Facility, the Australian Institute for Bioengineering and Nanotechnology, and the University of Queensland.
Author contributions (CRediT)
ACB: Conceptualization, Investigation, Writing, Visualization, Reviewing and Editing.
DRR: Conceptualization, Investigation, Writing, Visualization, Reviewing and Editing. CLP: Editing. YYL: Editing. VT: Editing. SH: Editing. EM: Editing. CBH: Editing. BLS: Reviewing and Editing
Notes
1 Active enzymes are denoted by the suffix “a” [Citation3].