Clonal selection of high producing, stably transfected HEK293 cell lines utilizing modified, high-throughput FACS screening

Journal of Chemical Technology and Biotechnology

Volumn 86, Issue 7, 2011, Pages 935-941

  Song, Michael ^a   Raphaelli, Kristin ^a   Jones, Martina L ^a   Aliabadi Zadeh, Khosrow ^a   Leung, Kar Man ^a   Crowley, David ^a   Hughes, Benjamin ^a   Mahler, Stephen ^a   Gray, Peter P ^a   Huang, Edwin P ^a   Chin, David Y ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Cold capture; FACS; HEK 293; Monoclonal antibody; Stable transfection

Indexed keywords

BAG PRODUCTION; BIOPHARMACEUTICALS; CELL SURFACES; CHINESE HAMSTER OVARY CELLS; CLONAL SELECTION; CLONAL SELECTION METHOD; COLD CAPTURE; EXPRESSION SYSTEM; FACS; FED BATCHES; FED-BATCH PRODUCTION; FEEDING REGIME; GRAM QUANTITIES; HEK-293; HEK293 CELLS; HIGH-THROUGHPUT; MAMMALIAN CELLS; PRECLINICAL DEVELOPMENT; RECOMBINANT ANTIBODY; RECOMBINANT PROTEIN; SECRETED PROTEIN; SPECIFIC PRODUCTIVITY; STABLE TRANSFECTION; THERAPEUTIC PROTEIN; TRANSIENT EXPRESSION; VOLUMETRIC OUTPUT;

BOTTLES; CELL CULTURE; CELL MEMBRANES; CLONING; FLOW CYTOMETRY; LAKES; MAMMALS; MONOCLONAL ANTIBODIES; PROTEINS; THROUGHPUT;

CLONE CELLS;

PROTEIN HYDROLYSATE; RECOMBINANT ANTIBODY;

ANTIBIOTIC RESISTANCE; ANTIBODY PRODUCTION; ANTIBODY TITER; ARTICLE; CELL CLONE; CELL ISOLATION; CELL STRAIN HEK293; CELL SURFACE; DRUG MANUFACTURE; DRUG PURIFICATION; EMBRYO; FED BATCH CULTURE; FLOW CYTOMETRY; FLUORESCENCE ACTIVATED CELL SORTING; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; MOLECULAR CLONING; PRODUCTIVITY; PROTEIN EXPRESSION; PROTEIN SECRETION;

CRICETULUS GRISEUS; MAMMALIA;

EID: 79958750588     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.2618     Document Type: Article

References (32)

1. Aggarwal S, What's fueling the biotech engine-2008. Nat Biotechnol 27: 987-993 (2009).
2. Beck A, Wurch T, Bailly C and Corvaia N, Strategies and challenges for the next generation of therapeutic antibodies. Nat Rev Immunol 10: 345-352 (2010).
3. Sheridan C, Fresh from the biologic pipeline-2009. Nat Biotechnol 28: 307-310 (2010).
4. Reichert JM, Rosensweig CJ, Faden LB and Dewitz MC. Monoclonal antibody successes in the clinic. Nat Biotechnol 23: 1073-1078 (2005).
5. Durocher Y and Butler M, Expression systems for therapeutic glycoprotein production. Curr Opin Biotechnol 20: 700-707 (2009).
6. Butler M, Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals. Appl Microbiol Biotechnol 68: 283-291 (2005).
7. Wurm FM, Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol 22: 1393-1398 (2004).
8. Chu L and Robinson DK, Industrial choices for protein production by large-scale cell culture. Curr Opin Biotechnol 12: 180-187 (2001).
9. Hansel TT, Kropshofer H, Singer T, Mitchell JA and George AJT, The safety and side effects of monoclonal antibodies. Nat Rev Drug Discov 9: 325-338 (2010).
10. Backliwal G, Hildinger M, Chenuet S, Wulhfard S, De Jesus M and Wurm FM, Rational vector design and multi-pathway modulation of HEK293E cells yield recombinant antibody titers exceeding 1g/L by transient transfection under serum-free conditions. Nucleic Acids Res 36: e96 (2008).
11. Sun X, Goh PE, Wong KT, Mori T and Yap MG, Enhancement of transient gene expression by fed-batch culture of HEK 293 EBNA1 cells in suspension. Biotechnol Lett 28: 843-848 (2006).
12. Kim KS, Kim MS Moon JH, Jeong MS, Kim J, Lee GM, et al, Enhancement of recombinant antibody production in HEK 293E cells by WPRE. Biotechnol Bioprocess Eng 14: 633-638 (2009).
13. Girod PA, Nguyen DQ, Calabrese D, Puttini S, Grandjean M, Martinet D, et al, Genome-wide prediction of matrix attachment regions that increase gene expression in mammalian cells. Nat Methods 4: 747-753 (2007).
14. Le Ru A, Jacob D, Transfiguracion J, Ansorge S, Henry O and Kamen AA, Scalable production of influenza virus in HEK-293 cells for efficient vaccine manufacturing. Vaccine 28: 3661-3671 (2010).
15. Thomas P and Smart TG, HEK293 cell line: a vehicle for the expression of recombinant proteins. J Pharmacol Toxicol Methods 51: 187-200 (2005).
16. Hacker DL, De Jesus M and Wurm FM, 25 years of recombinant proteins from reactor-grown cells-where do we go from here? Biotechnol Adv 27: 1023-1027 (2009).
17. Matasci M, Hacker DL, Baldi L and Wurm FM Recombinant therapeutic protein production in cultivated mammalian cells: current status and future prospects. Drug Discovery Today: Technol 5: e37-e42 (2008).
18. Hasse R, Argyros O, Wong SP, Harbottle RP, Lipps HJ, Ogris M, et al, pEPito: a significantly improved non-viral episomal expression vector for mammalian cells. BMC Biotechnol 10: 2033 (2010).
19. Browne SM and Al-Rubeai M, Selection methods for high-producing mammalian cell lines. Trends Biotechnol 25: 425-432 (2007).
20. Lindgren K, Salmen A, Lundgren M, Bylund L, Ebler A, Faldt E, et al, Automation of cell line development. Cytotechnology 59: 1-10 (2009).
21. Pechhold S, Stouffer M, Walker G, Martel R, Seligmann B, Hang Y, et al, Transcriptional analysis of intracytoplasmically stained FACS-purified cells by high-throughput, quantitative nuclease protection. Nat Biotechnol 27: 1038-1042 (2009).
22. Battye FL, Light A and Tarlinton DM, Single cell sorting and cloning. J Immunol Methods 243: 25-32 (2000).
23. Daugherty PS, Iverson BL and Georgiou G, Flow cytometric screening of cell-based libraries. J Immunol Methods 243: 211-227 (2000).
24. Pilbrough W, Munro TP and Gray P, Intraclonal protein expression heterogeneity in recombinant CHO cells. PLoS One 4: e8432 (2009).
25. Sleiman RJ, Gray PP, McCall MN, Codamo J and Sunstrom NA, Accelerated cell line development using two-color fluorescence activated cell sorting to select highly expressing antibody-producing clones. Biotechnol Bioeng 99: 578-587 (2008).
26. DeMaria CT, Cairns V, Schwarz C, Zhang J, Guerin M, Zuena E, et al, Accelerated clone selection for recombinant CHO CELLS using a FACS-based high-throughput screen. Biotechnol Prog 23: 465-472 (2007).
27. Brezinsky SC, Chiang GG, Szilvasi A, Mohan S, Shapiro RI, MacLean A, et al, A simple method for enriching populations of transfected CHO cells for cells of higher specific productivity. J Immunol Methods 277: 141-155 (2003).
28. Lin S, Shen Z, Zha D, Sharkey N, Prinz B, Hamilton S, et al, Selection of Pichia pastoris strains expressing recombinant immunoglobulin G by cell surface labeling. J Immunol Methods 358: 66-74 (2010).
29. Pichler J, Hesse F, Wieser M, Kunert R, Galosy SS, Mott JE, et al, A study on the temperature dependency and time course of the cold capture antibody secretion assay. J Biotechnol 141: 80-83 (2009).
30. Weaver JL, Introduction to flow cytometry. Methods 21: 199-201 (2000).
31. O'Callaghan PM and James DC, Systems biotechnology of mammalian cell factories. Brief Funct Genomic Proteomic 7: 95-110 (2008).
32. O'Callaghan PM, McLeod J, Pybus LP, Lovelady CS, Wilkinson SJ, Racher AJ, et al, Cell line-specific control of recombinant monoclonal antibody production by CHO cells. Biotechnol Bioeng 106: 938-951 (2010).