综述 |
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用于重组抗体生产的细胞大规模培养技术 |
刘伯宁 |
华北制药集团新药研究开发有限责任公司 抗体药物研制国家重点实验室 石家庄 050015 |
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The Lasted Development of Large Scale Cell Culture Technology for Commercial Antibody Manufacture |
LIU Bo-ning |
New Drug Reaserch and Development Center, North China Pharmaceutical Group Corporation and State Key Laboratory of Antibody drug Reaserch and Development, Shijiazhuang 050015, China |
[1] Chartrain M, Chu L. Development and production of commercial therapeutic monoclonal antibodies in mammalian cell expression systems: An overview of the current upstream technologies. Current Pharmaceutical Biotechnology, 2008, 9(6): 447-467. [2] Huang Y M, Hu W, Rustandi E, et al. Maximizing productivity of cho cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment. Biotechnology Progress, 2010, 26(5): 1400-1410. [3] 刘伯宁. 治疗性抗体研究进展与抗体产业关键技术. 中国生物工程杂志, 2013,33(5):132-138. Liu B N. The progress of therapeutic antibody drug and the industrial key-technology of antibody production. China Biotechnoloy, 2013,33(5):132-138 . [4] DePalma A. Enhancement of cell culture techniques. Genetic Engineering & Biotechnology News, 2009, 29(18). [5] 刘伯宁. 用于重组抗体生产的细胞构建技术研究进展. 中国生物工程杂志, 2013,33(6):111-116. Liu B N. The technology progress of antibody-producing cell line development. China Biotechnoloy, 2013,33 (6):111-116. [6] Xing Z, Li Z, Chow V, et al. Identifying inhibitory threshold values of repressing metabolites in cho cell culture using multivariate analysis methods. Biotechnology Progress, 2008, 24(3): 675-683. [7] Li F, Vijayasankaran N, Shen A Y, et al. Cell culture processes for monoclonal antibody production. MAbs, 2010, 2(5): 466-479. [8] Whitford CJaW. Bioreactor chapter two: Bioreactor control. Bioprocess Int Supplement, 2007. [9] Hermes P A, Castro C D. A fully defined, fed-batch, recombinant NS0 culture process for monoclonal antibody production. Biotechnology Progress, 2010, 26(5): 1411-1416. [10] Burky J E, Wesson M C, Young A, et al. Protein-free fed-batch culture of non-gs NS0 cell lines for production of recombinant antibodies. Biotechnology and Bioengineering, 2007, 96(2): 281-293. [11] Chee F W D, Tin K W K, Tang G L, et al. Impact of dynamic online fed-batch strategies on metabolism, productivity and n-glycosylation quality in cho cell cultures. Biotechnology and Bioengineering, 2005, 89(2): 164-177. [12] Khattak S F, Xing Z, Kenty B, et al. Feed development for fed-batch cho production process by semisteady state analysis. Biotechnology Progress, 2010, 26(3): 797-804. [13] De Alwis D M, Dutton R L, Scharer J, et al. Statistical methods in media optimization for batch and fed-batch animal cell culture. Bioprocess Biosyst Eng, 2007, 30(2): 107-113. [14] Jardin B A, Montes J, Lanthier S, et al. High cell density fed batch and perfusion processes for stable non-viral expression of secreted alkaline phosphatase (seap) using insect cells: Comparison to a batch sf-9-bev system. Biotechnology and Bioengineering, 2007, 97(2): 332-345. [15] Wang L, Hu H, Yang J, et al. High yield of human monoclonal antibody produced by stably transfected drosophila schneider 2 cells in perfusion culture using wave bioreactor. Molecular Biotechnology, 2011,52(2):170-179. [16] Vermasvuori R, Hurme M. Economic comparison of diagnostic antibody production in perfusion stirred tank and in hollow fiber bioreactor processes. Biotechnology Progress, 2011, 27(6): 1588-1598. [17] Pollock J, Ho S V, Farid S S. Fed-batch and perfusion culture processes: Economic, environmental, and operational feasibility under uncertainty. Biotechnology and Bioengineering, 2012,110(1):206-219. [18] Konstantinov K, Goudar C, Ng M, et al. The "push-to-low"approach for optimization of high-density perfusion cultures of animal cells. Adv Biochem Eng Biotechnol, 2006, 101:75-98. [19] Yang J D, Angelillo Y, Chaudhry M, et al. Achievement of high cell density and high antibody productivity by a controlled-fed perfusion bioreactor process. Biotechnology and Bioengineering, 2000, 69(1): 74-82. [20] Kim B J, Diao J, Shuler M L. Mini-scale bioprocessing systems for highly parallel animal cell cultures. Biotechnology Progress, 2012, 28(3): 595-607. [21] Legmann R, Schreyer H B, Combs R G, et al. A predictive high-throughput scale-down model of monoclonal antibody production in cho cells. Biotechnology and Bioengineering, 2009, 104(6): 1107-1120. [22] Chen A, Chitta R, Chang D, et al. Twenty-four well plate miniature bioreactor system as a scale-down model for cell culture process development. Biotechnology and Bioengineering, 2009, 102(1): 148-160. [23] Vijayasankaran N, Li J, Shawley R, et al. Animal cell culture media. Encyclopedia of Industrial Biotechnology, 2009.1-15. [24] Paula Decaria A S, William W. Many considerations in selecting bioproduction culture media. Bioprocess Int, 2009(11):44-51. [25] Mosser M, Chevalot I, Olmos E, et al. Combination of yeast hydrolysates to improve cho cell growth and igg production. Cytotechnology, 2012,14(12). [26] Jordan M, Voisard D, Berthoud A, et al. Cell culture medium improvement by rigorous shuffling of components using media blending. Cytotechnology, 2013,65(1):31-40. [27] Gonzalez-Leal I J, Carrillo-Cocom L M, Ramirez-Medrano A, et al. Use of a plackett-burman statistical design to determine the effect of selected amino acids on monoclonal antibody production in cho cells. Biotechnology Progress, 2011, 27(6): 1709-1717. [28] Fan L, Zhao L, Sun Y, et al. A high-yielding, generic fed-batch process for recombinant antibody production of gs-engineered cell lines. J Microbiol Biotechnol, 2009, 19(12): 1695-1702. [29] Xie L, Wang D I. Stoichiometric analysis of animal cell growth and its application in medium design. Biotechnology and Bioengineering, 1994, 43(11): 1164-1174. [30] Zhou W, Rehm J, Hu W S. High viable cell concentration fed-batch cultures of hybridoma cells through on-line nutrient feeding. Biotechnology and Bioengineering, 1995, 46(6): 579-587. [31] Fletcher T. Designing culture media for recombinant protein production:a rational approach. Bioprocess Int, 2005,3(1):30-36. [32] Zhou Jiang K D, Zhaohui Geng, Susan Casnocha, Zhihua Xiao, Steve Gorfien, and Scott J. Jacobia. Fed-batch cell culture process optimization: A rationally integrated approach. Bioprocess Int, 2012, 10(3): 40-45. [33] Min Zhang A L, Kerry K, Terrell J, et al. Rapid development and optimization of cell culture media. BioPharm International, 2008, 21(1):60-68. [34] Hammett K, Kuchibhatla J, Hunt C, et al. Developing chemically defined media through doe: Complete optimization with increased protein production in less than 8 months cell technology for cell products. 2007, 683-691. [35] Efren Pacis N V, Jincai L i, Martin G, et al. Systematic approaches to develop chemically defined cell culture feed media: It is important to ensure that the transition from peptone-containing to cd media doesn't affect product quality. BioPharm International Supplements, 2010, 23(11):22-32. [36] Ningning Ma J E, Centy O, Paul H, et al. A single nutrient feed supports both chemically defined ns0 and cho fed-batch processes: Improved productivity and lactate metabolism. Biotechnology Progress, 2009, 25(5):1353-1363. [37] Maranga L, Goochee C F. Metabolism of per.C6 cells cultivated under fed-batch conditions at low glucose and glutamine levels. Biotechnology and Bioengineering, 2006, 94(1): 139-150. [38] Kuwae S, Ohda T, Tamashima H, et al. Development of a fed-batch culture process for enhanced production of recombinant human antithrombin by chinese hamster ovary cells. Journal of Bioscience and Bioengineering, 2005, 100(5): 502-510. [39] Luo W, Sun X, Yi X, et al. Enhancement of hepatitis b surface antigen production by adenosine 5'-monophosphate in culture of recombinant chinese hamster ovary cells. Journal of Bioscience and Bioengineering, 2005, 100(4): 475-477. [40] Omasa T, Furuichi K, Iemura T, et al. Enhanced antibody production following intermediate addition based on flux analysis in mammalian cell continuous culture. Bioprocess Biosyst Eng, 2010, 33(1): 117-125. [41] Bai Y, Wu C, Zhao J, et al. Role of iron and sodium citrate in animal protein-free cho cell culture medium on cell growth and monoclonal antibody production. Biotechnology Progress, 2011, 27(1): 209-219. [42] Konno Y, Aoki M, Takagishi M, et al. Enhancement of antibody production by the addition of coenzyme-q(10). Cytotechnology, 2011, 63(2): 163-170. [43] Zhang J, Robinson D, Salmon P. A novel function for selenium in biological system: Selenite as a highly effective iron carrier for chinese hamster ovary cell growth and monoclonal antibody production. Biotechnology and Bioengineering, 2006, 95(6): 1188-1197. [44] deZengotita V M, Miller W M, Aunins J G, et al. Phosphate feeding improves high-cell-concentration ns0 myeloma culture performance for monoclonal antibody production. Biotechnology and Bioengineering, 2000, 69(5): 566-576. [45] Thombre S, Gadgil M. Increase in efficiency of media utilization for recombinant protein production in chinese hamster ovary culture through dilution. Biotechnology and Applied Biochemistry, 2011, 58(1): 25-31. [46] Chaderjian W B, Chin E T, Harris R J, et al. Effect of copper sulfate on performance of a serum-free cho cell culture process and the level of free thiol in the recombinant antibody expressed. Biotechnol Prog, 2005, 21(2): 550-553. [47] Qian Y, Khattak S F, Xing Z, et al. Cell culture and gene transcription effects of copper sulfate on chinese hamster ovary cells. Biotechnology Progress, 2011,27(4):1190-1194. [48] Schatz S M, Kerschbaumer R J, Gerstenbauer G, et al. Higher expression of fab antibody fragments in a cho cell line at reduced temperature. Biotechnology and Bioengineering, 2003, 84(4): 433-438. [49] Yoon S K, Song J Y, Lee G M. Effect of low culture temperature on specific productivity, transcription level, and heterogeneity of erythropoietin in chinese hamster ovary cells. Biotechnology and Bioengineering, 2003, 82(3): 289-298. [50] Yoon S K, Choi S L, Song J Y, et al. Effect of culture ph on erythropoietin production by chinese hamster ovary cells grown in suspension at 32.5 and 37.0 degrees c. Biotechnology and Bioengineering, 2005, 89(3): 345-356. [51] Sauer P W, Burky J E, Wesson M C, et al. A high-yielding, generic fed-batch cell culture process for production of recombinant antibodies. Biotechnology and Bioengineering, 2000, 67(5): 585-597. [52] Wu M H, Dimopoulos G, Mantalaris A, et al. The effect of hyperosmotic pressure on antibody production and gene expression in the gs-ns0 cell line. Biotechnology and Applied Biochemistry, 2004, 40(Pt 1): 41-46. [53] Shen D, Kiehl T R, Khattak S F, et al. Transcriptomic responses to sodium chloride-induced osmotic stress: A study of industrial fed-batch cho cell cultures. Biotechnology Progress, 2010, 26(4): 1104-1115. [54] Jiang Z, Sharfstein S T. Sodium butyrate stimulates monoclonal antibody over-expression in cho cells by improving gene accessibility. Biotechnology and Bioengineering, 2008, 100(1): 189-194. [55] Liu C, Chu I, Hwang S. Pentanoic acid, a novel protein synthesis stimulant for chinese hamster ovary (cho) cells. Journal of Bioscience and Bioengineering, 2001, 91(1): 71-75. [56] Backliwal G, Hildinger M, Kuettel I, et al. Valproic acid: A viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures. Biotechnology and Bioengineering, 2008, 101(1): 182-189. [57] Chun B H, Park S Y, Chung N, et al. Enhanced production of recombinant b-domain deleted factor viii from chinese hamster ovary cells by propionic and butyric acids. Biotechnology Letters, 2003, 25(4): 315-319. [58] Ling W L, Deng L, Lepore J, et al. Improvement of monoclonal antibody production in hybridoma cells by dimethyl sulfoxide. Biotechnology Progress, 2003, 19(1): 158-162. [59] Balcarcel R R, Stephanopoulos G. Rapamycin reduces hybridoma cell death and enhances monoclonal antibody production. Biotechnology and Bioengineering, 2001, 76(1): 1-10. [60] Qian Y, Jing Y, Li Z J. Glucocorticoid receptor-mediated reduction of igg-fusion protein aggregation in chinese hamster ovary cells. Biotechnology Progress, 2010, 26(5): 1417-1423. [61] Jing Y, Qian Y, Li Z J. Sialylation enhancement of ctla4-ig fusion protein in chinese hamster ovary cells by dexamethasone. Biotechnology and Bioengineering, 2010, 107(3): 488-496. [62] Rouiller Y, Perilleux A, Marsaut M, et al. Effect of hydrocortisone on the production and glycosylation of an fc-fusion protein in cho cell cultures. Biotechnology Progress, 2012, 28(3): 803-813. [63] Allen M J, Boyce J P, Trentalange M T, et al. Identification of novel small molecule enhancers of protein production by cultured mammalian cells. Biotechnology and Bioengineering, 2008, 100(6): 1193-1204. [64] Eon-Duval A, Broly H, Gleixner R. Quality attributes of recombinant therapeutic proteins: An assessment of impact on safety and efficacy as part of a quality by design development approach. Biotechnology Progress, 2012, 28(3): 608-622. [65] Walsh G, Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nature Biotechnology, 2006, 24(10): 1241-1252. [66] Swann P G, Tolnay M, Muthukkumar S, et al. Considerations for the development of therapeutic monoclonal antibodies. Curr Opin Immunol, 2008, 20(4): 493-499. [67] Schiestl M, Stangler T, Torella C, et al. Acceptable changes in quality attributes of glycosylated biopharmaceuticals. Nature Biotechnology, 2011, 29(4): 310-312. [68] Vazquez-Rey M, Lang D A. Aggregates in monoclonal antibody manufacturing processes. Biotechnology and Bioengineering, 2011, 108(7): 1494-1508. [69] Gomez N, Subramanian J, Ouyang J, et al. Culture temperature modulates aggregation of recombinant antibody in cho cells. Biotechnology and Bioengineering, 2012, 109(1): 125-136. [70] Ying Jinga M B, Samiksha Nayakb, Susan Egana, Yueming Qiana, Shih-Hsie Pana, Zheng Jian Lia. Identification of cell culture conditions to control protein aggregation of igg fusion proteins expressed in chinese hamster ovary cells. Process Biochemistry, 2012, 47(1): 69-75. [71] Jing Y, Qian Y, Ghandi M, et al. A mechanistic study on the effect of dexamethasone in moderating cell death in chinese hamster ovary cell cultures. Biotechnology Progress, 2012, 28(2): 490-496. [72] Trexler-Schmidt M, Sargis S, Chiu J, et al. Identification and prevention of antibody disulfide bond reduction during cell culture manufacturing. Biotechnology and Bioengineering, 2010, 106(3): 452-461. [73] Kao Y H, Hewitt D P, Trexler-Schmidt M, et al. Mechanism of antibody reduction in cell culture production processes. Biotechnol Bioeng, 2010, 107(4): 622-632. [74] Robert F, Bierau H, Rossi M, et al. Degradation of an fc-fusion recombinant protein by host cell proteases: Identification of a cho cathepsin d protease. Biotechnology and Bioengineering, 2009, 104(6): 1132-1141. [75] Kshirsagar R, McElearney K, Gilbert A, et al. Controlling trisulfide modification in recombinant monoclonal antibody produced in fed-batch cell culture. Biotechnology and Bioengineering, 2012, 109(10): 2523-2532. [76] Raju T S, Jordan R E. Galactosylation variations in marketed therapeutic antibodies. MAbs, 2012, 4(3):385-391. [77] Read E K, Park J T, Brorson K A. Industry and regulatory experience of the glycosylation of monoclonal antibodies. Biotechnology and Applied Biochemistry, 2011, 58(4): 213-219. [78] Hossler P, Khattak S F, Li Z J. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology, 2009, 19(9): 936-949. [79] Yuk I H, Zhang B, Yang Y, et al. Controlling glycation of recombinant antibody in fed-batch cell cultures. Biotechnology and Bioengineering, 2011, 108(11): 2600-2610. [80] Pacis E, Yu M, Autsen J, et al. Effects of cell culture conditions on antibody n-linked glycosylation-what affects high mannose 5 glycoform. Biotechnology and Bioengineering, 2011,108(10):2348-2358. [81] Malphettes L, Freyvert Y, Chang J, et al. Highly efficient deletion of fut8 in cho cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies. Biotechnology and Bioengineering, 2010, 106(5): 774-783. [82] Zhou Q, Shankara S, Roy A, et al. Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function. Biotechnology and Bioengineering, 2008, 99(3): 652-665. [83] Borys M C, Dalal N G, Abu-Absi N R, et al. Effects of culture conditions on n-glycolylneuraminic acid (neu5gc) content of a recombinant fusion protein produced in cho cells. Biotechnology and Bioengineering, 2010, 105(6): 1048-1057. [84] Gramer M J, Eckblad J J, Donahue R, et al. Modulation of antibody galactosylation through feeding of uridine, manganese chloride, and galactose. Biotechnology and Bioengineering, 2011, 108(7): 1591-1602. [85] Khawli L A, Goswami S, Hutchinson R, et al. Charge variants in igg1: Isolation, characterization, in vitro binding properties and pharmacokinetics in rats. MAbs, 2010, 2(6): 613-624. [86] Kaschak T, Boyd D, Lu F, et al. Characterization of the basic charge variants of a human igg1: Effect of copper concentration in cell culture media. MAbs, 2011, 3(6): 577-583. [87] Luo J, Zhang J, Ren D, et al. Probing of c-terminal lysine variation in a recombinant monoclonal antibody production using chinese hamster ovary cells with chemically defined media. Biotechnology and Bioengineering, 2012, 109(9): 2306-2315. [88] Khetan A, Huang Y M, Dolnikova J, et al. Control of misincorporation of serine for asparagine during antibody production using cho cells. Biotechnology and Bioengineering, 2010, 107(1): 116-123. [89] Wen D, Vecchi M M, Gu S, et al. Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in chinese hamster ovary cells. J Biol Chem, 2009, 284(47): 32686-32694. [90] Seamans T C, Beck A, Wurch T, et al. Cell cultivation process transfer and scale-up:in support of production of early clinical supplies of an anti igf-1r antibody, part 1. BioProcess International, 2008, 26-36. [91] Seamans T C, Beck A, Wurch T, et al. Cell cultivation processtransfer and scale-up:in support of production of early clinical supplies of an anti igf-1r antibody, part 2. BioProcess International, 2008, 34-42. [92] Xing Z, Kenty B M, Li Z J, et al. Scale-up analysis for a cho cell culture process in large-scale bioreactors. Biotechnology and Bioengineering, 2009, 103(4): 733-746. [93] Yang J D, Lu C, Stasny B, et al. Fed-batch bioreactor process scale-up from 3-l to 2,500-l scale for monoclonal antibody production from cell culture. Biotechnology and Bioengineering, 2007, 98(1): 141-154. [94] Abu-Absi S F, Yang L, Thompson P, et al. Defining process design space for monoclonal antibody cell culture. Biotechnology and Bioengineering, 2010, 106(6): 894-905. [95] Looby M, Ibarra N, Pierce J J, et al. Application of quality by design principles to the development and technology transfer of a major process improvement for the manufacture of a recombinant protein. Biotechnology Progress, 2011, 27(6): 1718-1729. [96] Rathore A S, Winkle H. Quality by design for biopharmaceuticals. Nat Biotechnol, 2009, 27(1): 26-34. [97] Dietmair S, Nielsen L K, Timmins N E. Mammalian cells as biopharmaceutical production hosts in the age of omics. Biotechnology Journal, 2012, 7(1): 75-89. [98] Read E K, Park J T, Shah R B, et al. Process analytical technology (pat) for biopharmaceutical products: Part i. Concepts and applications. Biotechnology and Bioengineering, 2010, 105(2): 276-284. [99] Teixeira A P, Oliveira R, Alves P M, et al. Advances in on-line monitoring and control of mammalian cell cultures: Supporting the pat initiative. Biotechnology Advances, 2009, 27(6): 726-732. |
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