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Appropriate mammalian expression systems for biopharmaceuticals

R G Werner1, W Noé, K Kopp

  • 1Boehringer Ingelheim Pharma KG, Biberach an der Riss, Germany.

Arzneimittel-Forschung
|September 28, 1998
PubMed
Summary

Mammalian cell expression systems and transgenic animals are evaluated for biopharmaceutical production. Chinese hamster ovary (CHO) cells and NSO-mouse myeloma cells show high expression titers, while transgenic animals offer greater overall yield for large quantities.

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Area of Science:

  • Biotechnology
  • Biopharmaceutical Manufacturing
  • Protein Expression Systems

Background:

  • Process development for biopharmaceuticals prioritizes product quality, safety, and manufacturing economy.
  • Mammalian cell expression systems, including CHO and NSO cells, and transgenic animals are key for producing pharmacologically active glycoproteins.
  • Expression titers depend on promoter constructs, integration sites, copy number, and protein type.

Purpose of the Study:

  • To evaluate mammalian cell expression systems and transgenic animals for biopharmaceutical production, focusing on expression titers, product yield, and glycosylation patterns.
  • To compare the effectiveness of different expression systems, specifically CHO and NSO cells versus transgenic animals, for producing monoclonal antibodies and recombinant proteins.
  • To assess the stability and influencing factors of protein glycosylation in different host cells and under various culture conditions.

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Main Methods:

  • Comparative analysis of expression titers and overall product yield across various mammalian cell lines (CHO, NSO) and transgenic animal systems.
  • Investigation of glycosylation patterns using analytical methods like peptide mapping, isoelectric focusing, oligosaccharide mapping, MALDI-TOF, capillary electrophoresis, and potency assays.
  • Experimental manipulation of culture conditions (e.g., process times, cultivation methods, ammonium ion concentration) to assess their impact on glycosylation.

Main Results:

  • CHO-NEOSPLA and NSO-GS systems are effective for monoclonal antibodies and recombinant proteins, with NSO cells yielding higher s-ICAM production than CHO cells.
  • Transgenic animals show the most promising overall product yield for proteins required in large quantities.
  • Glycosylation of proteins expressed in CHO cells was generally stable, with extreme conditions (process times, cultivation methods, ammonium concentration) influencing the profile. Tissue plasminogen activator (t-PA) exhibited the most stable glycosylation, while interferon omega and soluble intercellular adhesion molecule (s-ICAM) were more susceptible to changes.

Conclusions:

  • For high-quantity protein production, transgenic expression systems are attractive, whereas classical mammalian cell culture is preferred for low-quantity products where downstream processing dominates costs.
  • Protein glycosylation is critical for immunogenicity, activity, pharmacokinetics, solubility, and stability, and its pattern is influenced by host cell enzymatic systems and fermentation conditions.
  • The amino acid sequence of a protein influences its glycosylation pattern and sensitivity to culture conditions, necessitating careful selection of host cells and culture parameters to achieve desired glycosylation.