High-level expression of recombinant IgG in the human cell line PER.C6

David Jones, Nathalie Kroos, Regina Anema, Bart Van Montfort, Andre Vooys, Sven Van Der Kraats, Esmeralda Van Der Helm, Shirley Smits, Jan Schouten, Kirsten Brouwer, Fija Lagerwerf, Patrick Van Berkel, Dirk Jan Opstelten, Ton Logtenberg, Abraham Bout

Research output: Contribution to journalArticleAcademicpeer-review

98 Citations (Scopus)

Abstract

The number of therapeutic monoclonal antibodies in production is expected to rise rapidly in the next few years. As a result, there is much focus on the optimization of antibody expression platforms. Several issues are important including the speed of transition from bench to manufacturing, yield of IgG, and quality (particularly of the glycan structures present on immunoglobulins). We have characterized the human cell line PER.C6 for its ability to produce recombinant IgG. Production yields are still being optimized, but in nonfed batch culture, PER.C6 is able to grow to a cell density of 5 × 106 cells/mL and produce 300-500 mg/L IgG; this is likely to increase significantly in fed batch cultures. The generation of antibody-producing cell lines is fast, as rounds of amplification of inserted genes are not required for high production yields. The gene copy number of inserted genes is in the region of 1-10 copies per genome. In addition, PER.C6 is a human cell line, and so does not add glycans, which are immunogenic in humans. A core fucose molecule is essentially always present, and galactose residues are present at a physiological level (0, 1, and 2 galactose residues per glycan are present at a ratio of 1:2:1). No hybrid or high-mannose structures are seen.

Original languageEnglish
Pages (from-to)163-168
Number of pages6
JournalBiotechnology Progress
Volume19
Issue number1
DOIs
Publication statusPublished - 1 Jan 2003

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