TY - JOUR
T1 - High-level expression of recombinant IgG in the human cell line PER.C6
AU - Jones, David
AU - Kroos, Nathalie
AU - Anema, Regina
AU - Van Montfort, Bart
AU - Vooys, Andre
AU - Van Der Kraats, Sven
AU - Van Der Helm, Esmeralda
AU - Smits, Shirley
AU - Schouten, Jan
AU - Brouwer, Kirsten
AU - Lagerwerf, Fija
AU - Van Berkel, Patrick
AU - Opstelten, Dirk Jan
AU - Logtenberg, Ton
AU - Bout, Abraham
PY - 2003/1/1
Y1 - 2003/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0037277684&partnerID=8YFLogxK
U2 - 10.1021/bp025574h
DO - 10.1021/bp025574h
M3 - Article
C2 - 12573020
AN - SCOPUS:0037277684
SN - 8756-7938
VL - 19
SP - 163
EP - 168
JO - Biotechnology Progress
JF - Biotechnology Progress
IS - 1
ER -