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Name

SilenciO - Advanced Protein Expression by Galectin-1-Silencing

Organization name

PROvendis GmbH

Profile

Invention

Chinese Hamster ovary (CHO) cells are commonly used as a mammalian expression system for the production of recombinant proteins. They are one of the few cell types that can be grown at high cell density as the cells are resistant to metabolic stress.

The SilenciO-technology is a powerful tool for the expression of non-antibody proteins and antibodies suffering from an initially only poor expression rate

SilenciO-technology is based on a Galectin-1-knock down (>90%) by RNAi. This knock down reduces the metabolic load of the CHO expression system. The expression level of the protein of interest is increased by more than 1.5-fold.

Additional experiments revealed that using this method the yield of viable cells during fed-batch culture experiments is twice as high compared to control cells.

The level of host cell protein production is reduced by SilenciO-technology.

SilenciO-technology can be applied afterwards in all existing cell lines currently producing the protein with low and very low expression rates. Thus it enables the universal use for all protein drug candidates which are difficult to express and where the currently used manufacturing process leads to high cost-of-goods.

Commercial Opportunities

On behalf of the University Bielefeld, PROvendis offers non-exclusive licenses for commercial use (rights to this technology have already been granted to Boehringer Ingelheim).

Current Status

  • EP and US patent applications are pending.
  • Competitive Advantages
  • Enabling expression of sophisticated proteins (e.g. complex non-antibody proteins)
  • Reduction of host cell proteins
  • Increased yield of viable cells
  • Increased growth rate
  • Improved process robustness
  • Application in existing cell lines and bioprocesses

Further Reading

Krämer, O. (2014) RNAi-vermittelter knockdown zur Identifikation von Zielgenen für die Verbesserung von Produktionszelllinien. Dissertation, University of Bielefeld. Bielefeld 2014.

WO 2015/011172 „Method for recombinant protein production in mammalian cells“

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