Yeast-Made Human Enzyme: DNase1 Breakthrough
- A team at Ruhr University Bochum, led by Professor Beate Brand-Saberi, has successfully produced human DNase1 in yeast cells.
- DNase1,a protein that degrades cell-free DNA,has been used medically since 1958.
- To achieve this, researchers introduced the genetic information for human DNase1 into Pichia pastoris yeast cells.
A groundbreaking study reveals a new method for producing human DNase1, a critical enzyme in cystic fibrosis treatment, using yeast cells. This primarykeyword shift promises a more affordable and efficient production process, perhaps revolutionizing how we treat this and other conditions. Scientists at Ruhr University Bochum found that yeast cells can effectively synthesize the secondarykeyword protein, offering advantages over the current, more costly method of using hamster cells. This advancement could lead to wider accessibility of DNase1, which has also shown promise in treating conditions like sepsis and severe COVID-19. news Directory 3 reports on the cost-saving potential and expanded therapeutic applications. Discover what’s next as researchers optimize yeast production and explore new medical applications of this vital enzyme.
Yeast Cells Offer New Hope for Cystic Fibrosis Treatment
Updated April 29, 2025
A team at Ruhr University Bochum, led by Professor Beate Brand-Saberi, has successfully produced human DNase1 in yeast cells. this breakthrough, detailed in PLOS ONE, could pave the way for more affordable production of the protein, commonly used in cystic fibrosis treatment.
DNase1,a protein that degrades cell-free DNA,has been used medically since 1958. Currently, its production relies on costly and complex processes involving hamster cells. Dr. Markus Napirei, a researcher on the project, said producing human DNase1 with yeast offers advantages such as cost-effective culture conditions and rapid reproduction.
To achieve this, researchers introduced the genetic information for human DNase1 into Pichia pastoris yeast cells. These cells than integrated the information and released the protein. Jan-Ole Krischek, under the supervision of Napirei and Professor Hans Georg Mannherz, purified and characterized the human DNase1.
The team observed that the yeast produced less human DNase1 compared to mouse DNase1,despite the proteins sharing 82% of their structure. Napirei attributed this to differences in protein folding. Mouse DNase1 serves as a model for developing pharmacologically adapted human DNase1 isoforms.
In the body, DNase1 breaks down cell-free DNA in bodily fluids. in cystic fibrosis patients, DNA contributes to thick bronchial mucus. Inhaled DNase1 can liquefy this mucus,making it easier to cough up. The human enzyme DNase1 has been produced from ovary epithelial cells in hamsters and marketed since 1993.
DNase1’s potential extends beyond cystic fibrosis. It may help dissolve microthrombi containing DNA, which form during sepsis or severe COVID-19 infections.Clinical studies are also exploring its use in dissolving thrombosis in ischemic stroke patients.
What’s next
Further research will explore optimizing the yeast production process and investigating DNase1’s effectiveness in treating conditions involving excessive NET formation and microthrombi.