A platform for context-specific genetic engineering of recombinant protein production by CHO cells

Abbott, 2015, Optimisation of a simple method to transiently transfect a CHO cell line in high-throughput and at large scale, Protein Expr. Purif., 116, 113, 10.1016/j.pep.2015.08.016 Aggarwal, 2014, What’s fueling the biotech engine-2012 to 2013, Nat. Biotechnol., 32, 32, 10.1038/nbt.2794 Becker, 2008, An XBP-1 dependent bottle-neck in production of IgG subtype antibodies in chemically defined serum-free Chinese hamster ovary (CHO) fed-batch processes, J. Biotechnol., 135, 217, 10.1016/j.jbiotec.2008.03.008 Becker, 2010, Evaluation of a combinatorial cell engineering approach to overcome apoptotic effects in XBP-1(s) expressing cells, J. Biotechnol., 146, 198, 10.1016/j.jbiotec.2009.11.018 Birch, 2006, Antibody production, Adv. Drug Deliv. Rev., 58, 671, 10.1016/j.addr.2005.12.006 Borth, 2005, Effect of increased expression of protein disulfide isomerase and heavy chain binding protein on antibody secretion in a recombinant CHO cell line, Biotechnol. Prog., 21, 106, 10.1021/bp0498241 Brown, 2017, In silico design of context-responsive mammalian promoters with user-defined functionality, Nucleic Acids Res., 45, 10906, 10.1093/nar/gkx768 Brown, 2019, Whole synthetic pathway engineering of recombinant protein production, Biotechnol. Bioeng., 116, 375, 10.1002/bit.26855 Browne, 2007, Selection methods for high-producing mammalian cell lines, Trends Biotechnol., 25, 425, 10.1016/j.tibtech.2007.07.002 Cain, 2013, A CHO cell line engineered to express XBP1 and ERO1-L has increased levels of transient protein expression, Biotechnol. Prog., 29, 697, 10.1002/btpr.1693 Carlage, 2012, Analysis of dynamic changes in the proteome of a Bcl-XL overexpressing Chinese hamster ovary cell culture during exponential and stationary phases, Biotechnol. Prog., 28, 814, 10.1002/btpr.1534 Chong, 2010, Metabolomics-driven approach for the improvement of Chinese hamster ovary cell growth: overexpression of malate dehydrogenase II, J. Biotechnol., 147, 116, 10.1016/j.jbiotec.2010.03.018 Chung, 2004, Effect of doxycycline-regulated calnexin and calreticulin expression on specific thrombopoietin productivity of recombinant Chinese hamster ovary cells, Biotechnol. Bioeng., 85, 539, 10.1002/bit.10919 Cortez, 2014, The therapeutic potential of chemical chaperones in protein folding diseases, Prion, 8, 197, 10.4161/pri.28938 Daramola, 2014, A high-yielding CHO transient system: coexpression of genes encoding EBNA-1 and GS enhances transient protein expression, Biotechnol. Prog., 30, 132, 10.1002/btpr.1809 Davies, 2011, Impact of gene vector design on the control of recombinant monoclonal antibody production by chinese hamster ovary cells, Biotechnol. Prog., 27, 1689, 10.1002/btpr.692 Davies, 2012, Functional heterogeneity and heritability in CHO cell populations, Biotechnol. Bioeng., 110, 260, 10.1002/bit.24621 Davis, 2000, Effect of PDI overexpression on recombinant protein secretion in CHO cells, Biotechnol. Prog., 16, 736, 10.1021/bp000107q Dinnis, 2006, Functional proteomic analysis of GS-NS0 murine myeloma cell lines with varying recombinant monoclonal antibody production rate, Biotechnol. Bioeng., 94, 830, 10.1002/bit.20899 Doolan, 2008, Transcriptional profiling of gene expression changes in a PACE-transfected CHO DUKX cell line secreting high levels of Rhbmp-2, Mol. Biotechnol., 39, 187, 10.1007/s12033-008-9039-6 Duportet, 2014, A platform for rapid prototyping of synthetic gene networks in mammalian cells, Nucleic Acids Res., 42, 13440, 10.1093/nar/gku1082 Durose, 2006, Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress, Mol. Biol. Cell, 17, 3095, 10.1091/mbc.e06-01-0055 Fernandez-Martell, 2018, Metabolic phenotyping of CHO cells varying in cellular biomass accumulation and maintenance during fed-batch culture, Biotechnol. Bioeng., 115, 645, 10.1002/bit.26485 Fischer, 2015, The art of CHO cell engineering: a comprehensive retrospect and future perspectives, Biotechnol. Adv., 33, 1878, 10.1016/j.biotechadv.2015.10.015 Florin, 2009, Heterologous expression of the lipid transfer protein CERT increases therapeutic protein productivity of mammalian cells, J. Biotechnol., 141, 84, 10.1016/j.jbiotec.2009.02.014 Gutierrez, 2018, Genome-scale reconstructions of the mammalian secretory pathway predict metabolic costs and limitations of protein secretion, bioRxiv Hansen, 2015, Versatile microscale screening platform for improving recombinant protein productivity in Chinese hamster ovary cells, Sci. Rep., 5 Hansen, 2017, Improving the secretory capacity of Chinese hamster ovary cells by ectopic expression of effector genes: lessons learned and future directions, Biotechnol. Adv., 35, 64, 10.1016/j.biotechadv.2016.11.008 Harreither, 2015, Microarray profiling of preselected CHO host cell subclones identifies gene expression patterns associated with in-creased production capacity, Biotechnol. J., 10, 1625, 10.1002/biot.201400857 Huang, 2010, Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment, Biotechnol. Prog., 26, 1400, 10.1002/btpr.436 Hussain, 2018, A protein chimera strategy supports production of a model "difficult-to-express" recombinant target, FEBS Lett., 592, 2499, 10.1002/1873-3468.13170 Jayapal, 2007, Recombinant protein therapeutics from CHO cells - 20 years and counting, Cell Eng. Prog., 103, 40 Johari, 2015, Integrated cell and process engineering for improved transient production of a "difficult-to-express" fusion protein by CHO cells, Biotechnol. Bioeng., 112, 2527, 10.1002/bit.25687 Kaneyoshi, 2019, Secretion analysis of intracellular "difficult-to-express" immunoglobulin G (IgG) in Chinese hamster ovary (CHO) cells, Cytotechnology, 71, 305, 10.1007/s10616-018-0286-5 Kim, 2012, CHO cells in biotechnology for production of recombinant proteins: current state and further potential, Appl. Microbiol. Biotechnol., 93, 917, 10.1007/s00253-011-3758-5 Ku, 2008, Effects of overexpression of X-box binding protein 1 on recombinant protein production in Chinese hamster ovary and NS0 myeloma cells, Biotechnol. Bioeng., 99, 155, 10.1002/bit.21562 Kuo, 2018, The emerging role of systems biology for engineering protein production in CHO cells, Curr. Opin. Biotechnol., 51, 64, 10.1016/j.copbio.2017.11.015 Le Fourn, 2014, CHO cell engineering to prevent polypeptide aggregation and improve therapeutic protein secretion, Metab. Eng., 21, 91, 10.1016/j.ymben.2012.12.003 Lee, 2007, Improving the expression of a soluble receptor : fc fusion protein in CHO cells by coexpression with the receptor ligand, Cell Technol. Cell Prod., 10.1007/978-1-4020-5476-1_4 Lewis, 2013, Genomic landscapes of Chinese hamster ovary cell lines as revealed by the Cricetulus griseus draft genome, Nat. Biotechnol., 31, 10.1038/nbt.2624 Lund, 2017, Network reconstruction of the mouse secretory pathway applied on CHO cell transcriptome data, BMC Syst. Biol., 11 Mason, 2012, Identifying bottlenecks in transient and stable production of recombinant monoclonal-antibody sequence variants in chinese hamster ovary cells, Biotechnol. Prog., 28, 846, 10.1002/btpr.1542 Merquiol, 2011, HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response, PLoS One, 6 Mohan, 2010, Effect of inducible Co-overexpression of protein disulfide isomerase and endoplasmic reticulum oxidoreductase on the specific antibody productivity of recombinant chinese Hamster ovary cells, Biotechnol. Bioeng., 107, 337, 10.1002/bit.22781 Moore, 2012, The unfolded protein response in secretory cell function, Annu. Rev. Genet., 46, 165, 10.1146/annurev-genet-110711-155644 Mora, 2018, Sustaining an efficient and effective CHO cell line development platform by incorporation of 24-deep well plate screening and multivariate analysis, Biotechnol. Prog., 34, 175, 10.1002/btpr.2584 Nissom, 2006, Transcriptome and proteome profiling to understanding the biology of high productivity CHO cells, Mol. Biotechnol., 34, 125, 10.1385/MB:34:2:125 O’callaghan, 2010, Cell line-specific control of recombinant monoclonal antibody production by CHO cells, Biotechnol. Bioeng., 106, 938, 10.1002/bit.22769 O’callaghan, 2015, Diversity in host clone performance within a Chinese hamster ovary cell line, Biotechnol. Prog., 31, 1187, 10.1002/btpr.2097 Prashad, 2015, Dynamics of unfolded protein response in recombinant CHO cells, Cytotechnology, 67, 237, 10.1007/s10616-013-9678-8 Priola, 2016, High-throughput screening and selection of mammalian cells for enhanced protein production, Biotechnol. J., 11, 853, 10.1002/biot.201500579 Pybus, 2014, Model-directed engineering of "difficult-to-express" monoclonal antibody production by Chinese hamster ovary cells, Biotechnol. Bioeng., 111, 372, 10.1002/bit.25116 Rahimpour, 2013, Engineering the cellular protein secretory pathway for enhancement of recombinant tissue plasminogen activator expression in chinese Hamster ovary cells: effects of CERT and XBP1s genes, J. Microbiol. Biotechnol., 23, 1116, 10.4014/jmb.1302.02035 Rutkowski, 2004, A trip to the ER: coping with stress, Trends Cell Biol., 14, 20, 10.1016/j.tcb.2003.11.001 Rutkowski, 2006, Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins, PLoS Biol., 4, 2024, 10.1371/journal.pbio.0040374 Schlatter, 2005, On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells, Biotechnol. Prog., 21, 122, 10.1021/bp049780w Singer, 2007, To triplicate or not to triplicate?, Chemom. Intell. Lab. Syst., 86, 82, 10.1016/j.chemolab.2006.08.008 Smales, 2004, Comparative proteomic analysis of GS-NSO murine myeloma cell lines with varying recombinant monoclonal antibody production rate, Biotechnol. Bioeng., 88, 474, 10.1002/bit.20272 Sommeregger, 2016, Proteomic differences in recombinant CHO cells producing two similar antibody fragments, Biotechnol. Bioeng., 113, 1902, 10.1002/bit.25957 Tadauchi, 2019, Utilizing a regulated targeted integration cell line development approach to systematically investigate what makes an antibody difficult to express, Biotechnol. Prog., 35 Thompson, 2017, High-throughput quantitation of Fc-containing recombinant proteins in cell culture supernatant by fluorescence polarization spectroscopy, Anal. Biochem., 534, 49, 10.1016/j.ab.2017.07.013 Tigges, 2006, Xbp1-based engineering of secretory capacity enhances the productivity of Chinese hamster ovary cells, Metab. Eng., 8, 264, 10.1016/j.ymben.2006.01.006 Tirosh, 2005, XBP-1 specifically promotes IgM synthesis and secretion, but is dispensable for degradation of glycoproteins in primary B cells, J. Exp. Med., 202, 505, 10.1084/jem.20050575 Torella, 2014, Rapid construction of insulated genetic circuits via synthetic sequence-guided isothermal assembly, Nucleic Acids Res., 42, 681, 10.1093/nar/gkt860 Walter, 2011, The unfolded protein response: from stress pathway to homeostatic regulation, Science, 334, 1081, 10.1126/science.1209038 Wlaschin, 2007, Engineering cell metabolism for high-density cell culture via manipulation of sugar transport, J. Biotechnol., 131, 168, 10.1016/j.jbiotec.2007.06.006 Wurm, 2004, Production of recombinant protein therapeutics in cultivated mammalian cells, Nat. Biotechnol., 22, 1393, 10.1038/nbt1026 Wurm, 2011, First CHO genome, Nat. Biotechnol., 29, 718, 10.1038/nbt.1943 Yee, 2009, Comparative transcriptome analysis to unveil genes affecting recombinant protein productivity in mammalian cells, Biotechnol. Bioeng., 102, 246, 10.1002/bit.22039