Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Bailey KM (2008) Balancing the need for speed during development of early-stage clinical versus late-stage commercial antibody processes. Optimising Biomanufacturing Processes (oral presentation)
Bebbington C, Renner G, Thomson S et al (1992) High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker. Nat Biotech 10:169–175
Benton T, Chen T, McEntee M et al (2002) The use of UCOE vectors in combination with a preadapted serum free suspension cell line allows for rapid production of large quantities of protein. Cytotechnol 38:43–46
Bianchi A, McGrew J (2003) High-level expression of full-length antibodies using trans-complementing expression vectors. Biotechnol Bioeng 84(4):439–444
Bosques C, Collins B, Meador J et al (2010) Chinese Hamster Ovary cells can produce galactose-α-1,3-galactose antigens on proteins. Nat Biotechnol 28(11):1153–1156
Brezinsky S, Chiang G, Szilvasi A et al (2003) A simple method for enriching populations of transfected CHO cells for cells of higher specific productivity. J Immunol Methods 277:141–155
Burgess D (2013) Technology: a CRISPR genome-editing tool. Nat Rev Genet 14(2):80
Cabaniols J, Paques F (2008) Robust cell line development using meganucleases. Methods Mol Biol 435:31–45
Cairns V, DeMaria C, Poulin F et al (2011) Utilization of non-AUG initiation codons in a flow cytometric method for efficient selection of recombinant cell lines. Biotechnol Bioeng 108(11):2611–2622
Campbell M, Corisdeo S, McGee C, Kraichely D (2010) Utilization of site-specific recombination for generating therapeutic protein producing cell lines. Mol Biotechnol 45:199–202
Caron A, Nicolas C, Gaillet B et al (2009) Fluorescent labeling in semi-solid medium for selection of mammalian cells secreting high-levels of recombinant proteins. BMC Biotechnol 9:42
Christian M, Cermak T, Doyle E et al (2010) Targeting DNA double-strand breaks with TAL effector nucleases. Genetics 186(2):757–761
Chung C, Mirakhur B, Chan E et al (2008) Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose. N Engl J Med 358(11):1109–1117
Clarke C, Henry M, Doolan P, Kelly S, Aherne S, Sanchez N, Kelly P, Kinsella P, Breen L, Madden SF, Zhang L, Leonard M, Clynes M, Meleady P, Barron N (2012) Integrated miRNA, mRNA and protein expression analysis reveals the role of post-transcriptional regulation in controlling CHO cell growth rate. BMC Genomics 13:656
Cockett M, Bebbington C, Yarranton G (1991) The use of engineered E1A genes to transactivate the hCMV-MIE promoter in permanent CHO cell lines. Nucleic Acids Res 19(2):319–325
Coffman JL, Kramarczyk JF, Kelley BD (2008) High-throughput screening of chromatographic separations: I. Method development and column modeling. Biotech Bioeng 100(4):605–618
Combs RG, Yu E, Roe S et al (2011) Fed-batch bioreactor performance and cell line stability evaluation of the artificial chromosome expression technology expressing an IgG1 in Chinese hamster ovary cells. Biotechnol Prog 27(1):201–208
Doolan P, Melville M, Gammell P, Sinacore M, Meleady P, McCarthy K, Francullo L, Leonard M, Charlebois T, Clynes M (2008) Transcriptional profiling of gene expression changes in a PACE-transfected CHO DUKX cell line secreting high levels of rhBMP-2. Mol Biotechnol 39(3):187–199
DeMaria C, Cairns V, Schwarz C et al (2007) Accelerated clone selection for recombinant CHO cells using a FACS based high throughput screen. Biotechnol Prog 23(2):465–472
Deetz JS (2008) Realizing the vision of biology over steel: Wyeth BioPharma’s strategy for platform process development. The 236th ACS National Meeting (Oral presentation)
Essers R, Kewes H, Schiedner G (2011) Improving volumetric productivity of a stable human CAP cell line by bioprocess optimization. BMC Proc 5(Suppl 8):66
Fan L, Kadura I, Krebs L et al (2012) Improving the efficiency of CHO cell line generation using glutamine synthetase gene knockout cells. Biotechnol Bioeng 109(4):1007–1015
Ferrara C, Brunker P, Suter T et al (2006) Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnol Bioeng 93(5):851–861
Figueroa B, Ailor E, Osborne D et al (2007) Enhanced cell culture performance using inducible anti-apoptotic genes E1B-19K and Aven in the production of a monoclonal antibody with Chinese hamster ovary cells. Biotechnol Bioeng 97(4):877–892
Gammell P, Barron N, Kumar N, Clynes M (2007) Initial identification of low temperature and culture stage induction of miRNA expression in suspension CHO-K1 cells. J Biotechnol 130(3):213–218
Ghaderi D, Taylor R, Padler-Karavani V et al (2010) Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat Biotechnol 28(8):863–867
Girod PA, Nguyen DQ, Calabrese D, Puttini S, Grandjean M, Martinet D, Regamey A, Saugy D, Beckmann JS, Bucher P, Mermod N (2007) Genome-wide prediction of matrix attachment regions that increase gene expression in mammalian cells. Nat Methods 4(9):747–753
Grandjean M, Girod P-A, Calabrese D, Kostyrko K, Wicht W, Yerly F, Mazza C, Beckmann JS, Martinet D, Mermod N (2011) High-level transgene expression by homologous recombination-mediated gene transfer. Nuc Acids Res 39(15):e104
Haines A (2012) Use of islands of automation for cell line development. IBC Cell Line Dev & Eng
Hammond S, Kaplarevic M, Borth N, Betenbaugh MJ, Lee KH (2012) Chinese hamster genome database: an online resource for the CHO community at www.CHOgenome.org. Biotechnol Bioeng 109(6):1353–1356
Houston JG, Banks MN, Binnie A, Brenner S, O’Connell J, Petrillo EW (2008) Case study: impact of technology investment on lead discovery at Bristol-Myers Squibb, 1998–2006. Drug Disc Today 13(1/2):44–51
Huang Y, Li Y, Wang YG, Gu X, Wang Y, Shen BF (2007) An efficient and targeted gene integration system for high-level antibody expression. J Immunol Methods 322:28–39
Huggett B, Lahteenmaki R (2012) Public biotech 2011-the numbers. Nat Biotechnol 30(8):751–757
Jadhav V, Hackly M, Bort J et al (2012) screening method to assess biological effects of microRNA overexpression in Chinese hamster ovary cells. Biotechnol Bioeng 109(6):1376–1385
Jones D, Kroos N, Anema R et al (2003) High-level expression of recombinant IgG in the human cell line per.c6. Biotechnol Prog 19(1):163–168
Kanda Y, Imai-Nishiya H, Kuni-Kamochi R et al (2007) Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: a new strategy for generating completely non-fucosylated recombinant therapeutics. J Biotechnol 130(3):300–310
Kanda Y, Yamane-Ohnuki N, Sakai N et al (2006) Comparison of cell lines for stable production of fucose-negative antibodies with enhanced ADCC. Biotechnol Bioeng 94(4):680–688
Kennard ML, Goosney DL, Monteith D, Zhang L, Moffat M, Fischer D, Mott J (2009) The generation of stable, high MAb expressing CHO cell lines based on the Artificial Chromosome Expression (ACE) technology. Biotech Bioeng 104(3):540–553
Kim JY, Kim Y-G, Lee GM (2012) CHO cells in biotechnology for production of recombinant proteins: current state and further potential. Appl Microbiol Biotechnol 93:917–930
Kito M, Itami S, Fukano Y, Yamana K, Shibui T (2002) Construction of engineered CHO strains for high-level production of recombinant proteins. Appl Microbiol Biotechnol 60:442–448
Kober L, Zehe C, Bode J (2012) Development of a novel ER stress based selection system for the isolation of highly productive clones. Biotechnol Bioeng 109(10):2599–2611
Kramer O, Klausing S, Noll T (2010) Methods in mammalian cell line engineering: from random mutagenesis to sequence-specific approaches. Appl Microbiol Biotechnol 88:425–436
Kwaks T, Barnett P, Hemrika W et al (2003) Identification of anti-repressor elements that confer high and stable protein production in mammalian cells. Nat Biotechnol 21(5):553–558
Lee E, Roth J, Paulson J (1989) Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of beta-galactoside alpha 2,6-sialyltransferase. J Biol Chem 264(23):13848–13855
Lee K, Jin X, Zhang K et al (2003) A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease. Glycobio 13(4):305–313
Lee Y, Wong K, Tan J et al (2009) Overexpression of heat shock proteins (HSPs) in CHO cells for extended culture viability and improved recombinant protein production. J Biotechnol 143:34–43
Legman R, Schreyer HB, Combs RG, McCormick EL, Russo AP, Rodgers ST (2009) A predictive high-throughput scale-down model of monoclonal antibody production in CHO cells. Biotech Bioeng 104(6):1107–1120
Lindenbaum M, Perkins E, Csonka E et al (2004) A mammalian artificial chromosome engineering system (ACE System) applicable to biopharmaceutical protein production, transgenesis, and gene-based cell therapy. Nuc Acids Res 32(21):e172
Liu P, Chan E, Cost G et al (2010) Generation of a triple-gene knockout mammalian cell line using engineered zinc-finger nucleases. Biotechnol Bioeng 106(1):97–105
Llop E, Gutierrez-Gallego R, Segura J et al (2008) Structural analysis of the glycosylation of gene-activated erythropoietin (epoetin delta, Dynepo). Anal Biocehm 383:243–254
Meng Y, Liang J, Wong W et al (2000) Green fluorescent protein as a second selectable marker for selection of high producing clones from transfected CHO cells. Gene 242:201–207
Mohan C, Kim Y, Koo J, Lee G (2008) Assessment of cell engineering strategies for improved therapeutic protein production in CHO cells. Biotechnol J 3(5):624–630
Nagy A (2000) Cre recombinase: the universal reagent for genome tailoring. Genesis 26:99–109
Nehlsen K, Schucht R, de Gamma-Norton L, Krömer W, Baer A, Cayli A, Hauser H, Wirth D (2009) Recombinant protein expression by targeting pre-selected chromosomal loci. BMC Biotechnol 9:100
Nieminen M, Tuuri T, Savilahti H (2010) Genetic recombination pathways and their application for genome modification of human embryonic stem cells. Exp Cell Res 316(16):2578–2586
Noguchi A, Mukuria C, Suzuki E et al (1995) Immunogenicity of N-glycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese Hamster Ovary Cells. J Biochem 117(1):59–62
Paulin RP, Ho T, Balzer HJ, Holliday R (1998) Gene silencing by DNA methylation and dual inheritance in Chinese Hamster Ovary Cells. Genetics 149:1081–1088
Prajapati S (2012) High-throughput analytical platforms for cell line and process development. IBC 9th bioprocess international conference and exhibition
Prentice H, Ehrenfels B, Sisk W (2007) Improving performance of mammalian cells in fed-batch processes through “bioreactor evolution”. Biotechnol Prog 23:458–464
Russell J (2012) Improving cell culture optimization. Gen Eng Biotechnol News 32(7)
Schlake T, Bode J (1994) Use of mutated FLP recognition target (FRT) sites for the exchange of expression cassettes at defined chromosomal loci. Biochem 33(43):12746–12751
Shahrokh Z, Royle L, Saldova R et al (2011) Erythropoietin produced in a human cell line (Dynepo) has significant differences in glycosylation compared with erythropoietins produced in CHO cell lines. Mol Pharm 8(1):286–296
Shields R, Lai J, Keck R et al (2002) Lack of fucose on human IgG1N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 277(300):26733–26740
Sinacore MS, Drapeau D, Adamson SR (1999) Adaptation of mammalian cells to growth in serum-free media. Animal Cell Biotech: Methods Biotech 8:11–22
Sleiman R, Gray P, McCall M et al (2008) Accelerated cell line development using two-color fluorescence activated cell sorting to select highly expressing antibody-producing clones. Biotechnol Bioeng 99(3):578–587
Tabuchi H, Sugiyama T (2013) Cooverexpression of alanine aminotransferase 1 in Chinese hamster ovary cells overexpressing taurine transporter further stimulates metabolism and enhances product yield. Biotechnol Bioeng
Tan H, Lee M, Yap M, Wang D (2008) Overexpression of cold-inducible RNA-binding protein increases interferon-gamma production in Chinese-hamster ovary cells. Biotechnol Appl Biocem 49:247–257
Tummala S, Titus M, Wilson L et al (2012) Evaluation of exogenous siRNA addition as a metabolic engineering tool for modifying biopharmaceuticals. Biotechnol Prog
Urlaub G, Chasin L (1980) Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity. Proc Natl Acad Sci 77:4216–4220
van Blockland H, Kwaks T, Sewalt R et al (2007) A novel high stringency selection system allows screening of few clones for high protein expression. J Biotechnol 128(2):237–245
von Horsten H, Ogorek C, Blanchard V et al (2010) Production of non-fucosylated antibodies by co-expression of heterologous GDP-6-deoxy-D-lyxo-4-hexulose reductase. Glycobiol 20(12):1607–1618
Wang Z, Gerstein M, Snyder M (2009) RNA-Seq: a revolutionary tool for transcriptomics. Nat Rev Genet 10(1):57–63
Westwood A, Rowe D, Clarke H (2010) Improved recombinant protein yield using a codon deoptimized DHFR selectable marker in a CHEF1 expression plasmid. Biotechnol Prog 26(6):1558–1566
Wong D, Wong K, Nissom P et al (2006) Targeting early apoptotic genes in batch and fed-batch CHO cell cultures. Biotechnol Bioeng 95(3):350–361
Xu X, Nagarajan H, Lewis N et al (2011) The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line. Nat Biotechnol 29:735–741
Yamane-Ohnuki N, Kinoshita S, Inoue-Urakubo M et al (2004) Establishment of FUT8 knockout Chinese Hamster Ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol Bioeng 87(5):614–622
Yee JC, de Leon GM, Philp RJ, Yap M, Hu WS (2008) Genomic and proteomic exploration of CHO and hybridoma cells under sodium butyrate treatment. Biotech Bioeng 99(5):1186–1204
Zahn-Zabal M, Kobr M, Girod P et al (2001) Development of stable cell lines for production or regulated expression using matrix attachment regions. J Biotechnol 87(1):29–42
Zhang M, Koskie K, Ross J et al (2010) Enhancing glycoprotein sialylation by targeted gene silencing in mammalian cells. Biotechnol Bioeng 105(6):1094–1105
Zhang P, Haryadi R, Chan K et al (2012) Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant. Glycobiology 22(7):897–911
Zhou M, Crawford Y, Ng D et al (2011) Decreasing lactate level and increasing antibody production in Chinese Hamster Ovary cells (CHO) by reducing the expression of lactate dehydrogenase and pyruvate dehydrogenase kinases. J Biotechnol 153:27–34
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Estes, S., Melville, M. (2013). Mammalian Cell Line Developments in Speed and Efficiency. In: Zhou, W., Kantardjieff, A. (eds) Mammalian Cell Cultures for Biologics Manufacturing. Advances in Biochemical Engineering/Biotechnology, vol 139. Springer, Berlin, Heidelberg. https://doi.org/10.1007/10_2013_260
Download citation
DOI: https://doi.org/10.1007/10_2013_260
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-54049-3
Online ISBN: 978-3-642-54050-9
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)