Mammalian cell protein expression for biopharmaceutical production

Biotechnology Advances

Volumn 30, Issue 5, 2012, Pages 1158-1170

  Zhu, Jianwei ^a  

^a SAIC FREDERICK INC   (United States)

Author keywords

Biopharmaceutical development; Mammalian cell; Manufacturing; Protein expression

Indexed keywords

ACTIVE AREA; ANALYTICAL METHOD; BIOPHARMACEUTICAL DEVELOPMENT; CELL LINES; CHINESE HAMSTER OVARY CELLS; CLINICAL APPLICATION; CLINICAL DEVELOPMENT; CULTURE CONDITIONS; DEVELOPMENT STAGES; EXPRESSION SYSTEM; GENE SILENCING; GENE TARGETING; GENETIC MECHANISM; IMPACT FACTOR; MAMMALIAN CELLS; POST-TRANSLATIONAL MODIFICATIONS; PRODUCT QUALITY; PROTEIN EXPRESSIONS; RECOMBINANT PROTEIN PRODUCTIONS; TECHNOLOGY PLATFORMS; TRANSIENT GENE EXPRESSIONS;

CELL ENGINEERING; GENE EXPRESSION; GENETIC ENGINEERING; GLYCOLS; MANUFACTURE; RECOMBINANT PROTEINS;

ANIMAL CELL CULTURE;

RECOMBINANT PROTEIN;

CELL ORGANELLE; DEVELOPMENTAL BIOLOGY; DOMINANCE; DRUG; GENE EXPRESSION; MAMMAL; MOLECULAR ANALYSIS; PROTEIN; RECOMBINATION;

ANIMAL; ARTICLE; BIOSYNTHESIS; CELLS; GENE EXPRESSION; GLYCOSYLATION; HUMAN; MAMMAL; METABOLISM; METHODOLOGY; PHARMACEUTICS;

ANIMALS; BIOPHARMACEUTICS; CELLS; GENE EXPRESSION; GLYCOSYLATION; HUMANS; MAMMALS; RECOMBINANT PROTEINS;

CRICETULUS GRISEUS; MAMMALIA;

EID: 84862541940     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2011.08.022     Document Type: Article

References (170)

1. Akinc A., Thomas M., Klibanov A.M., Langer R. Exploring polyethylenimine-mediated DNA transfection and the proton sponge hypothesis. J Gene Med 2004, 7:657-663.
2. Aldrrich T.L., Viaje A., Morris A.E. EASE vectors for rapid stable expression of recombinant antibodies. Biotechnol Prog 2003, 19:1433-1438.
3. Allen M.J., Boyce J.P., Trentalange M.T., Treiber D.L., Rasmussen B., Tillotson B., et al. Identification of novel small molecule enhancers of protein production by cultured mammalian cells. Biotechnol Bioeng 2008, 100:1193-1204.
4. Altamirano C., Paredes C., Illanes A., Cairo J.J., Godia F. Strategies for fed-batch cultivation of t-PA producing CHO cells: substitution of glucose and glutamine and rational design of culture medium. J Biotechnol 2004, 110:171-179.
5. Andersen D.C., Goochee C.F. The effect of cell-culture conditions on the oligosaccharide structure of secreted glycoproteins. Curr Opin Biotechnol 1994, 5:546-549.
6. Andersen D.C., Krummen L. Recombinant protein expression for therapeutic applications. Curr Opin Biotechnol 2002, 13:117-123.
7. Backliwal G., Hildinger M., Chenuet S., Wulhfard S., Jesus M.D., Wurm F.M. Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions. Nucleic Acids Res 2008, 36(e96):1-7.
8. Backliwal G., Hildinger M., Hasija V., Wurm F.M. High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a prior DNA complex formation with PEI. Biotechnol Bioeng 2008, 99:721-727.
9. Bai Y., Wu C., Zhao J., Liu Y.H., Ding W., Ling W.L.W. Role of iron and sodium citrate in animal protein-free CHO cell culture medium on cell growth and monoclonal antibody production. Biotechnol Prog 2011, 27:209-219.
10. Baldi L., Hacker D.L., Adam M., Wurm F.M. Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives. Biotechnol Lett 2007, 29:677-684.
11. Batard P., Jordan M., Wurm F.M. Transfer of high copy number plasmid into mammalian cells by calcium phosphate transfection. Gene 2001, 270:61-68.
12. Bebbington C.R., Renner G., Thomson S., King D., Abrams D., Yarranton G.T. High level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable maker. Biotechnology 1992, 10:169-175.
13. Beck A., Wagner-Rousset E., Bussat M.C., Lokteff M., Klinguer-Hamour C., Haeuw J.F., et al. Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and Fc-fusion proteins. Curr Pharm Biotechnol 2008, 9:421-422.
14. Benton T., Chen T., McEntee M., Fox B., King D., Crombie R., et al. The use of UCOE vectors in combination with a preadapted serum free, suspension cell line allows for rapid production of large quantities of protein. Cytotechnology 2002, 38:43-46.
15. Bergamaschi C., Rosati M., Jalah R., Valentin A., Kulkarni V., Alicea C., et al. Intracellular interaction of interleukin-15 with its receptor a during production leads to mutual stabilization and increased bioactivity. J Biol Chem 2008, 283:4189-4199.
16. Bergamaschi C., Jalah R., Kulkarni V., Rosati M., Zhang G.M., Alicea C., et al. Secretion and biological activity of short signal peptide IL-15 is chaperoned by IL-15 receptor alpha in vivo. J Immunol 2009, 183:3064-3072.
17. Birch J.R., Racher A.J. Antibody production. Adv Drug Deliv Rev 2006, 58:671-685.
18. Bork K., Horstlorte R., Weidemann W. Increasing the sialylation of therapeutic glycoproteins: the potential of the sialic acid biosynthetic pathway. J Pharm Sci 2009, 98:3499-3508.
19. Boussif O. A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine. Proc Natl Acad Sci U S A 1995, 92:7297-7301.
20. Bulleid N.J., Bassel-Duby R.S., Freedman R.B., Sambrook J.F., Gething M.J. Cell-free synthesis of enzymically active tissue-type plasminogen activator. Protein folding determines the extent of N-linked glycosylation. Biochem J 1992, 286(Pt 1):275-280.
21. Butler M. Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals. Appl Microbiol Biotechnol 2005, 68:283-291.
22. Cacciatore J.J., Chasin L.A., Leonard E.F. Gene amplification and vector engineering to achieve rapid and high-level therapeutic protein production using the Dhfr-based CHO cell selection system. Biotechnol Adv 2010, 28:673-681.
23. Carnes A.E., Luke J.M., Vincent J.M., Schular A., Anderson S., Hodgson C.P., et al. Plasmid DNA fermentation strain and process-specific effects on vector yield, quality and transgene expression. Biotechnol Bioeng 2011, 108:354-363.
24. Castro P.M., Ison A.P., Hayter P.M., Bull A.T. The macroheterogeneity of recombinant human interferon-gamma produced by Chinese-hamster ovary cells is affected by the protein and lipid content of the culture medium. Biotechnol Appl Biochem 1995, 21(Pt 1):87-100.
25. Cheng L., Sun X., Yi X., Zhang Y. Large-scale plasmid preparation for transient gene expression. Biotechnol Lett 2011, 33:1559-1564.
26. Chiang G.G., Sisk W.P. Bcl-x(L) mediates increased production of humanized monoclonal antibodies in Chinese hamster ovary cells. Biotechnol Bioeng 2005, 91:779-792.
27. Cho M.S., Yee H., Brown C., Jeang K.T., Chan S. An oriP expression vector containing the HIV-1 Tat/TAR transactivation axis produces high levels of protein expression in mammalian cells. Cytotechnology 2001, 37:23-30.
28. Cho M.S., Yee H., Brown C., Mei B., Mirenda C., Chan S. Versatile expression system for rapid and stable production of recombinant proteins. Biotechnol Prog 2003, 19:229-232.
29. Clincke M.-F., Guedon E., Yen F.T., Ogier V., Roitel O., Goergen J.-L. Effect of surfactant Pluronic F-68 on CHO cell growth, metabolism, production, and glycosylation of human recombinant IFN-γ in mid operating conditions. Biotechnol Prog 2011, 27:181-190.
30. Crowell C.K., Grampp G.E., Rogers G.N., Miller J., Scheinman R.I. Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system. Biotechnol Bioeng 2007, 96:538-549.
31. Cruz H.J., Peixoto C.M., Nimtz M., Alves P.M., Dias E.M., Moreira J.L., et al. Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells. Biotechnol Bioeng 2000, 69:129-139.
32. Darby N. Trends in biological manufacturing. ASME: 2nd Annual Bioprocess Technology Seminars & Exhibition - Europe 2008, http://www.asmeconferences.org/bioprocesseurope08/ASMEDarby.pdf.
33. Deer J.R., Allison D.S. High-level expression of proteins in mammalian cells using transcription regulatory sequences from the Chinese hamster EF1-α gene. Biotechnol Prog 2004, 20:880-889.
34. Derouazi M., Girard P., Tiborgh F.V., Iglesias K., Muller N., Bertschinger M., et al. Serum-free largescale transient transfection of CHO cells. Biotechnol Bioeng 2004, 87:537-545.
35. Ding S., Wu X., Li G., Han M., Zhang Y., Xu T. Efficient transposition of the piggyback (PB) transposon in mammalian cells and mice. Cell 2005, 122:473-483.
36. Dorai H., Nemeth J.F., Cammaart E., Wang Y., Tang Q.M., Magill A., et al. Development of mammalian production cell lines expressing CNTO736, a glucagon like peptide-1-MIMETIBODY: factors that influence productivity and product quality. Biotechnol Bioeng 2009, 103:162-176.
37. Dorai H., Kyung Y.S., Ellis D., Kinney C., Lin C., Jan D., et al. Expression of anti-apoptosis genes alters lactate metabolism of Chinese Hamster Ovary cells in culture. Biotechnol Bioeng 2009, 103:592-608.
38. Dorai H., Ellis D., Keung Y.S., Campbell M., Zhuang M., Lin C., et al. Combining high-throughput screening of caspase activity with anti-apoptosis genes for development of robust CHO production cell lines. Biotechnol Prog 2010, 26:1367-1381.
39. Durocher Y., Butler M. Expression system for therapeutic glycoprotein production. Curr Opin Biotechnol 2009, 20:700-707.
40. Durocher Y., Sylvie Perret S., Kamen A. High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res 2002, 30(e9):1-7.
41. Ehrhardt C., Schmolke M., Matzke A., Knoblauch A., Will C., Wixler V., et al. Polyethylenimine, a cost-effective transfection reagent. Signal Transduct 2006, 6:179-184.
42. Eichacker P.Q., Natanson C., Danner R.L. Surviving sepsis-practice guideline, marketing campaigns, and Eli Lilly. N Engl J Med 2006, 355:1640-1642.
43. Florin L., Lipske C., Becker E., Kaufmann H. Supplementation of serum free media with HT is not sufficient to restore growth properties of DHFR-/- cells in fed-batch processes-Implications for designing novel CHO-based expression platforms. J Biotechnol 2011, 152:189-193.
44. Franco R., Daniela G., Fabrizio M., Ilaria G., Detlev H. Influence of osmolarity and pH increase to achieve a reduction of monoclonal antibodies aggregates in a production process. Cytotechnology 1999, 29:11-25.
45. Franconi R., Demurtas O.C., Massa S. Plant-derived vaccines and other therapeutics produced in contained systems. Expert Rev Vaccines 2010, 9:877-892.
46. Gagnon M., Hiller G., Luan Y.-T., Kittredge A., DeFelice J., Drapeau D. High-end pH-controlled delivery of glucose effectively suppresses lactate accumulation in CHO fed-batch cultures. Biotechnol Bioeng 2011, 108:1328-1337.
47. Gawlitzek M., Valley U., Nimtz M., Wagner R., Conradt H.S. Characterization of changes in the glycosylation pattern of recombinant proteins from BHK-21 cells due to different culture conditions. J Biotechnol 1995, 29:117-131.
48. Gawlitzek M., Ryll T., Lofgren J., Sliwkowski M.B. Ammonium alters N-glycan structures of recombinant TNFR-IgG: Degradative versus biosynthetic mechanisms. Biotechnol Bioeng 2000, 68:637-646.
49. Geisse S., Fux C. Recombinant protein production by transient gene transfer into mammalian cells. Methods in Enzymology. Volume 463: Guide to protein purification 2009, 223-238. 463. 2nd edition. R.R. Burgess, M.P. Deutscher (Eds.).
50. Geisse S., Jordan M., Wurm F.M. Large-scale transient expression of therapeutic protein in mammalian cells. Methods in Molecular Biology, vol 308: Therapeutic Proteins: Methods and Protocols 2005, 87-98. Humana Press Inc., Totowa, NJ. C.M. Smales, D.C. James (Eds.).
51. Global Biotechnology Market Review & World Top Ten Biotech Drugs World Top Companies, Medicinal Brands, Biologics and Market Trends http://knol.google.com/k/krishan-maggon/global-biotechnology-market-review/3fy5eowy8suq3/16.
52. Godbey W.T., Wu K.K., Mikos A.G. Tracking the intracellular path of poly(ethylenimine)/DNA complexes for gene delivery. Proc Natl Acad Sci 1999, 96:5177-5181.
53. Guo D., Gao A., Michels D.A., Feeney L., Eng M., Chan B., et al. Mechanism of unintended amino acid sequence changes in recombinant monoclonal antibodies expressed in Chinese Hamster Ovary (CHO) cells. Biotechnol Bioeng 2010, 107:163-171.
54. Hahn T.J., Goochee C.F. Growth-associated glycosylation of transferrin secreted by HepG2 cells. J Biol Chem 1992, 267:23982-23987.
55. Harcum S.W. Chapter 5. Protein Glycosylation. Cell Culture Technology for Pharmaceutical and Cell-Based Therapies 2006, 113-153. S.S. Ozturk, W.-S. Hu (Eds.).
56. Hayter P.M., Curling E.M., Gould M.L., Baines A.J., Jenkins N., Salmon I., et al. The effect of the dilution rate on CHO cell physiology and recombinant interferon-gamma production in glucose-limited chemostat culture. Biotechnol Bioeng 1993, 42:1077-1085.
57. Heidemann R., Lunse S., Tran D., Zhang C. Characterization of cell-banking parameters for the cryopreservation of mammalian cell lines in 100-mL cryobags. Biotechnol Prog 2010, 26:1154-1163.
58. Hong W.W., Wu S.C. A novel RNA silencing vector to improve antigen expression and stability in Chinese hamster ovary cells. Vaccine 2007, 25:4103-4111.
59. Hossler P., Khattak S.F., Li Z.J. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 2009, 19:936-949.
60. Huang W. The shrinking biomanufacturing facility. GEN 2005, 25(42-4):6.
61. Huang Y., Li Y., Wang Y.G., Gu X., Wang Y., Shen B.F. An efficient and targeted gene integration system for high-level antibody expression. J Immunol Methods 2007, 322:28-39.
62. Huang Y.-M., Hu W.W., Rustandi E., Chang K., Yusuf-Makagiansar H. Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment. Biotechnol Prog 2010, 26:1400-1410.
63. Jalah R., Rosati M., Kulkarni V., Patel V., Bergamaschi C., Valentin A., et al. Efficient system expression of bioactive IL-15 in Mice upon delivery of optimized DNA expression plamsid. DNA Cell Biol 2007, 26:827-840.
64. Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 2005, 21:11-16.
65. Jenkins N., Castro P., Menon S., Ison A., Bull A. Effect of lipid supplements on the production and glycosylation of recombinant interferon-gamma expressed in CHO cells. Cytotechnology 1994, 15:209-215.
66. Junker B. Challenges in biopharmaceutical scale-up to production. Advanced in biopharmaceutical manufacturing and scale-up production 2007, 287-328. 2nd edition. E.S. Langer (Ed.).
67. Kaneko Y., Sato R., Aoyagi H. Changes in the quality of antibodies produced by Chinese hamster ovary cells during the death phase of cell culture. J Biosci Bioeng 2010, 109:281-287.
68. Kennard M.L. Engineered mammalian chromosomes in cellular protein production: future prospects. Methods Mol Biol 2011, 738:217-238.
69. Khetan A., Huang Y.M., Dolnikova J., Pederson N.E., Wen D., Yusuf-Makagiansar H., et al. Control of misincorporation of serine for asparagine during antibody production using CHO cells. Biotechnol Bioeng 2010, 107:116-123.
70. Kim S.H., Lee G.M. Down-regulation of lactate dehydrogenase-A by siRNAs for reduced lactic acid formulation of Chinese hamster ovary cells producing thrombopoietin. Appl Microbiol Biotechnol 2007, 74:152-159.
71. Kim K.-S., Kim M.S., Moon J.H., Jeong M.S., Kim J., Lee G.M., et al. Enhancement of recombinant antibody production in HEK 293E cells by WPRE. Biotechnol Bioprocess Eng 2009, 14:633-638.
72. Kim H.Y., Tsai S., Lo S.C., Wear D.J., Izadjoo M.J. Production and characterization of chimeric monoclonal antibodies against Burkholderia pseudomallei and B. Mallei using the DHFR expression system. PLoS One 2011, 6(e19867):1-14. http://www.plosone.org.
73. Kim M., O'Callaghan P.M., Droms K.A., James D.C. A mechanistic understanding of production instability in CHO cell lines expressing recombinant monoclonal antibodies. Biotechnol Bioeng 2011, May 2. [Epub ahead of print]. 10.1002/bit.23189.
74. Klebanoff C.A., Finkelstein S.E., Surman D.R., Lichtman M.K., Gattinoni L., Theoret M.R., et al. IL-15 enhances the in vivo antitumor activity of tumor-reactive CD8+ T cells. Proc Natl Acad Sci U S A 2004, 101:1969-1974.
75. Kochanowski N., Blanchard F., Cacan R., Chirt F., Guedon E., Marc A., et al. Influence of intracellular nucleotide and nucleotide suger contents on recombinant interferon-g glycosylation during batch and fed-batch culture of CHO cells. Biotechnol Bioeng 2008, 100:721-733.
76. Kotsopoulou E., Bosteels H., Chim Y.T., Pegman P., Stephen G., Thornhill S.I., et al. Optimised mammalian eexpresion through the coupling of codon adaptation with gene amplification: maximum yields with minimum effort. J Biotechnol 2010, 146:186-193.
77. Krampe B., Al-Rubeai Cell death in mammalian cell culture: molecular mechanisms and cell line engineering strategies. Cytotechnology 2010, 62:175-188.
78. Kruif J.D., Kramer A., Nijhuis R., Zande V.V.D., Blanken R.D., Clements C., et al. Generation of stable cell clones expressing mixtures of human antibodies. Biotechnol Bioeng 2010, 106:741-750.
79. Kunkel J.P., Jan D.C., Jamieson J.C., Butler M. Dissolved oxygen concentration in serum-free continuous culture affects N-linked glycosylation of a monoclonal antibody. J Biotechnol 1998, 62:55-71.
80. Kunkel J.P., Jan D.C., Butler M., Jamieson J.C. Comparisons of the glycosylation of a monoclonal antibody produced under nominally identical cell culture conditions in two different bioreactors. Biotechnol Prog 2000, 16:462-470.
81. Lao M.-S., Toth D. Effects of ammonium and lactate on growth and metabolism of a recombinant Chinese hamster ovary cell culture. Biotechnol Prog 1997, 13:688-691.
82. Li B., Ryan P.W., Ray B.H., Leister K.J., Sirmuthu N.M., Ryder A.G. Rapid characterization and quality control of complex cell culture media solutions using raman spectroscopy and chemometrics. Biotechnol Bioeng 2010, 107:290-301.
83. Lida S., Misaka H., Inoue M., Shibata M., Nakano R., Yamane-Ohnuki N., et al. Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa. Clin Cancer Res 2006, 12:2879-2888.
84. Lu Y., Williamson B., Gillespie R. Recent advancement in application of hydrophobic interaction chromatography for antibody aggregate removal in industrial purification process. Curr Pharm Biotechnol 2009, 10:427-433.
85. 'Mac' Cheever M.A. Twelve immunotherapy drugs that could cure cancers. Immunol Rev 2008, 222:357-368.
86. Mahmoud K. Recombinant protein production: strategic technology and a vital research tool. Res J Cell Mol Biol 2007, 1:9-22.
87. Majors B.S., Betenbaug M.J., Pederson N.E., Chiang G.G. Enhancement of transient gene expression and culture viability using Chinese hamster ovary cells overexpressing Bcl-xL. Biotechnol Bioeng 2008, 101:567-578.
88. Maliyekkel A., Davis B.M., Roninson I.B. Cell cycle arrest drastically extends the duration of gene silencing after transient expression of short hairpin RNA. Cell Cycle 2006, 5:2390-2395.
89. Mammalian cell culture: protein technologies and market overview 2005, 100. Drug and Market Development Publishing, Sep. http://www.researchandmarkets.com.
90. Matasci M., Hacker D.L., Baldi L., Wurm F.M. Recombinant therapeutic protein production in cultivated mammalian cells: current status and future prospects. Drug Discov Today 2009, 10.1016/j.ddatec.2008.12.003.
91. Matasci M., Baldi L., Hacker D.L., Wurm F.M. The piggyBac tansposon enhances the frequency of CHO stable cell line generation and yields recombinant lines with superior productivity and stability. Biotechnol Bioeng 2011, 108:2141-2150.
92. Matin-Montanez E., Lopez-Tellez J.F., Acevedo M.J., Pavia J., Khan Z.U. Efficiency of gene transfection reagents in NG108-15, SH-SY5Y and CHO-K1 cell lines. Methods Find Exp Clin Pharmacol 2010, 32:291-297.
93. Meyer H.P., Brass J., Jungo C., Klein J., Wenger J., Mommers R. An emerging start for therapeutic and catalytic protein production. BioProcess Int 2008, 6:S10-S21.
94. Mohan C., Lee G.M. Effect of inducible co-overexpression of protein disulfide isomerase and endoplasmic reticulum oxidoreductase on the specific antibody productivity of recombinat Chinese hamster ovary cells. Biotechnol Bioeng 2010, 107:337-346.
95. Mohan C., Park S.H., Chung J.Y., Lee G.M. Effect of doxycycline regulated protein disulfide isomerase expression on the specific productivity of recombinant CHO cells: Thrombopoietin and antibody. Biotechnol Bioeng 2007, 983:611-615.
96. Morrow K.J. Optimizing transient gene expression. Applications expected to move beyond discovery and the preclinic to clinical realm. Genet Eng Biotechnol News 2008, 28(5). (March 1).
97. Mortier E., Quéméner A., Vusio P., Lorenzen I., Boublik Y., Grötzinger J., et al. Soluble interleukin-15 receptorα (IL-15Rα)-sushi as a selective and potent agonist of IL-15 action through IL-15Rβ/γ. J Biol Chem 2006, 281:1612-1619.
98. Muller N. Transient Gene Expression for Rapid Protein Production: Studies & Optimizations under Serum-Free Conditions. Dissertation 2005, http://biblion.epfl.ch/EPFL/theses/2005/3297/EPFL_TH3297.pdf.
99. Murhammer D.W., Goochee C.F. Structural features of nonionic polyglycol polymer molecules responsible for the protective effect in sparged animal cell bioreactor. Biotechnol Prog 1990, 95:39-48.
100. Muthing J., Kemminer S.E., Conradt H.S., Sagi D., Nimtz M., Karst U. Peter-Katalinic. Effects of buffering conditions and culture pH on production rates and glycosylation of clinical phase I anti-melanoma mouse IgG3 monoclonal antibody R24. Biotechnol Bioeng 2003, 83:321-334.
101. Nahrgang S., Kkagten E., Jesus D., Bourgeois M., Dejardin S., Von Stockar U. The effect of cell line, transferction procedure and reactor conditions on the glycosylation of recombinant human anti-Rhesus D IgG1. Animal Cell Technology: Products from Cells, Cells as Products. Proceeding of the 16th ESACT meeting 1999, April 25-29 Lugano Switzerland. A. Bernard (Ed.).
102. Nair A.R., Xie J., Hermiston T.W. Effect of different UCOE-promoter combinations in creation of engineered cell lines for the production of Factor VIII. BMC Res Notes 2011, 4:178.
103. Nivitchanyong T., Martinez A., Ishaque A., Murphy J.E., Konstantinov K., Betenbaugh M.J., et al. Anti-apoptotic genes Aven and E1B-19K enhance performance of BHK cells engineed to express recombinant factor VIII in batch and low perfusion cell culture. Biotechnol Bioeng 2007, 98:825-841.
104. Oberbek A., Matasci M., Hacker D.L., Wurm F.M. Generation of stable, high-producing CHO cell lines by lentiviral vector-mediated gene transfer in serum-free suspension culture. Biotechnol Bioeng 2011, 108:600-610.
105. Patel T.P., Parekh R.B., Moellering B.J., Prior C.P. Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody. Biochem J 1992, 285:839-845.
106. Pilbrough W., Munro T.P., Gray P. Intraclonal protein expression heterogeneity in recombinant CHO cells. PLoS One 2009, 4:e8432.
107. Pogue G.P., Vojdani F., Palmer K.E., Hiatt E., Hume S., Phelps J., et al. Production of pharmaceutical-grade recombinant aprotinin and a monoclonal antibody product using plant-based transient expression systems. Plant Biotechnol J 2010, 8:638-654.
108. Potter H., Weir L., Leder P. Enhancer-dependent expression of human κimmunoglobulin genes introduced into mouse pre-B lymphocytes by electroporation. Proc Natl Acad Sci U S A 1984, 81:7161-7165.
109. Primack J., Flynn G.C., Pan H. A high-throughput microchip-based glycan screening assay for antibody cell culture samples. Electrophoresis 2011, 32:1129-1132.
110. Rader R.A. FDA Biopharmaceutical Product Approvals and Trends http://www.biopharma.com.
111. Rajendra Y., Kiseljak D., Baldi L., David L., Hacker D.L., Wurm F.M. A simple high-yielding process for transient gene expression in CHO cells. J Biotechnol 2011, 153:22-26.
112. Raymond C.S., Soriano P. High-efficiency FLP and PhiC31 site-specific recombination in mammalian cells. PLoS One 2007, 2:e162.
113. Redwan el-RM Animal-derived pharmaceutical proteins. J Immunoassay Immunochem 2009, 30:262-290.
114. L promoter of E. coli phage lambda. Gene 1981, 15:81-93.
115. Rhee W.J., Lee E.H., Park T.H. Expression of Bombyx mori 30Kc19 protein in Escherichia coli and its anti-apoptotic effect in Sf9 cell. Biotechnol Bioprocess Eng 2009, 14:645-650.
116. Rodrigues M.E., Costa A.R., Henriques M., Azeredo J., Oliveira R. Technological progresses in monoclonal antibody production systems. Biotechnol Prog 2010, 26:332-351.
117. Rodriguez J., Spearman M., Huzel N., Butler M. Enhanced production of monomeric interferon-beta by CHO cells through the control of culture conditions. Biotechnol Prog 2005, 21:22-30.
118. Rossi D.L., Rossi E.A., Goldenberg D.M., Chang C.-H. A new mammalian host cell with enhanced survival enables completely serum-free development of high-level protein production cell lines. Biotechnol Prog 2011, 27:766-775.
119. Rothman R.J., Warren L., Vliegenthart J.F., Hard K.J. Clonal analysis of the glycosylation of immunoglobulin G secreted by murine hybridomas. Biochemistry 1989, 28:1377-1384.
120. Rudolph C., Lausier J., Naundorf S., Müller R.H., Rosenecker J. In vivo gene delivery to the lung using polyethylenimine and fractured polyamidoamine dendrimers. J Gene Med 2000, 2:269-278.
121. Ruffoni B., Pistelli L., Bertoli A., Pistelli L. Plant cell cultures: bioreactors for industrial production. Adv Exp Med Biol 2011, 698:203-221.
122. Sambrook J., Russell D.W. Molecular Cloning. A Laboratory Manual 2001, 16.7-16.21. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, Volume 3.
123. Sasaki H., Bothner B., Dell A., Fukuda M. Carbohydrate structure pf erythropoietin expressed in Chinese Hamster Ovary cells by a human eruthropoietin cDNA. J Biol Chem 1987, 262:12059-12076.
124. Schirmer E.B., Kuczewski M., Golden K., Lain B., Bragg C., Chon J., et al. Primary clarification of very high-density cell culture harvests by enhanced cell settling. BioProcess Int 2010, 32-39. (January).
125. Seth G., Hossler P., Yee J.C., Hu W.S. Engineering cells for cell culture bioprocessing-physiological fundamentals. Adv Biochem Eng Biotechnol 2006, 101:119-164.
126. Shelikoff M., Sinskey A.J., Stephanopoulos G. The effect of protein synthesis inhibitors on the glycosylation site occupancy of recombinant human prolactin. Cytotechnology 1994, 5:195-208.
127. Shields R.L., Lai J., Keck R., O'Connell L.Y., Hong K., Meng Y.G., et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 2002, 277:26733-26740.
128. Shiloach J., Rinas U. Bacterial cultivation for production of proteins and other biological products. Manual of Industrial Microbiology and Biotechnology 2010, 132-144. 3rd edition. R.H. Baltz (Ed.).
129. Singer A., Eiteman M.A., Altman E. DNA plasmid production in different host strains of Escherichia coli. J Ind Microbiol Biotechnol 2009, 36:521-530.
130. Solomon A., Weiss D.T., Wall J.S. Therapeutic potential of chimeric amyloid-reactive monoclonal antibody 11-1F4. Clin Cancer Res 2003, 9:3831s-3838s.
131. Stettler M., Zhang X., Hacker D.L., Jesus M.D., Wurm F.M. Novel orbital shake bioreactors for transient production of CHO derived IgGs. Biotechnol Prog 2007, 23:1340-1346.
132. Suda E.J., Thomas K.E., Pabst T.M., Mensah P., Ramasubramanyan N., Gustafson M.E. Comparison of agarose and dextran-grafted agarose strong ion exchangers for the separation of protein aggregates. J Chromatogr A 2009, 1216:5256-5264.
133. Tait A.S., Brown C.J., Galbraith D.J., Hines M.J., Hoare M., Birch J.R., et al. Transient production of recombinant proteins by Chinese Hamster Ovary cells using polyethyleneimine/DNA complexes in combination with microtubule disrupting anti-mitotic agents. Biotechnol Bioeng 2004, 88:707-721.
134. Teague R.M., Sather B.D., Sacks J.A., Huang M.Z., Dossett M.L., Morimoto J., et al. Interleukin-15 rescues tolerant CD8+ T cells for use in adoptive immunotherapy of established tumors. Nat Med 2006, 12:335-341.
135. Thaisuchat H., Baumann M., Pontiller J., Hesse F., Ernst W. Identification of a novel temperature sensitive promoter in CHO cells. BMC Biotechnol 2011, 11(51). http://www.biomedcentral.com/1472-6750/11/51.
136. Tharmalingam T., Ghebeh H., Wuerz T., Butler M. Pluronic enhances the robustness and reduces the cell attachment of mammalian cells. Mol Biotechnol 2008, 39:167-177.
137. Thyagarajan B., Calos M.P. Site-specific integration for high-level protein production in mammalian cells. Methods Mol Biol 2005, 308:99-106.
138. Tiscornia G., Tergaonkar V., Galimi F., Verma I.M. CRE recombinase-inducible RNA interference mediated by lentiviral vectors. Proc Natl Acad Sci U S A 2004, 101:7347-7351.
139. Trummer E., Fauland K., Seidinger S., Schriebl K., Lattenmayer C., Kunert R., et al. Process parameter shifting: Part 1. Effect of DOT, pH, and temperature on the performance of Epo-Fc expressing CHO cells cultivated in controlled batch bioreactors. Biotechnol Bioeng 2006, 94:1033-1044.
140. Van Craenenbroeck K., Vanhoenacker P., Haegeman G. Episomal vectors for gene expression in mammalian cells. Eur J Biochem 2000, 267:5665-5678.
141. Vazquez-Rey M., Lang D.A. Aggregates in monoclonal antibody manufacturing process. Biotechnol Bioeng 2011, 108:1494-1508.
142. Walsh G. Biopharmaceutical benchmark 2006. Nat Biotechnol 2006, 24:769-776.
143. Wang L., Hale G., Ghosh R. Non-size-based membrane chromatographic separation and analysis of monoclonal antibody aggregates. Anal Chem 2006, 78:6863-6867.
144. Wang Z., Park J.H., Park H.H., Tan W., Park T.H. Enhancement of recombinant human EPO production and sialylation in chinese hamster ovary cells through expression. Biotechnol Bioeng 2011, 108:1634-1642.
145. Weikert S., Papac D., Briggs J., Cowfer D., Tom S., Gawlitzek M., et al. Engineering Chinese hamster ovary cells to maximize sialic acid content of recombinant glycoproteins. Nat Biotechnol 1999, 17:1116-1121.
146. Wen D., Vecchi M.M., Gu S., Su L., Dolnikova J., Huang Y.M., et al. Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in CHO cells. J Biol Chem 2009, 284:32686-32694.
147. Williams J.A., Luke J., Langtry S., Anderson S., Hodgson C.P., Carnes A.E. Generic plasmid DNA production platform incorporating low metabolic burden seed-stock and fed-batch fermentation process. Biotechnol Bioeng 2009, 103:1129-1143.
148. Wiznerowicz M., Trono D. Harnessing HIV for therapy, basic research and biotechnology. Trends Biotechnol 2005, 23:42-47.
149. Wong D.C.F., Wong K.T.K., Goh L.T., Heng C.K., Yap M.G.S. Impact of dynamic online fed-batch strategies on metabolism, productivity and N-glycosylation quality in CHO cell cultures. Biotechnol Bioeng 2005, 93:1005-1016.
150. Wong N.S., Yap M.G., Wang D.I. Enhancing recombinant glycoprotein sialation through CMP-sialic acid transporter over expression in Chinese hamster ovary cells. Biotechnol Bioeng 2006, 93:1005-1016.
151. Wong A.W., Baginski T.K., Reilly D.E. Enhancement of DNA uptake in FUT8-deleted CHO cells for transient production of afucosylated antibodies. Biotechnol Bioeng 2010, 106:751-763.
152. Wu S.C. RNA interference technology to improve recombinant protein production in Chinese hamster ovary cells. Biotechnol Adv 2009, 27:417-422.
153. Wu S.C., Meir Y.J., Coates C.J., Handler A.M., Pelczar P., Moisyadi S., et al. PiggyBac is a flexible and highly active transposon as compared to sleeping beauty, Tol2, and Mos1 in mammalian cells. Proc Natl Aced Sci U S A 2006, 103:15008-15013.
154. Wulhfard S., Tissot S., Bouchet S., Cevey J., Jesus M.D., Hacker D.L., et al. Mild hypothermia improves transient gene expression yields several fold in Chinese hamster ovary cells. Biotechnol Prog 2008, 24:458-465.
155. Wulhfard S., Baldi L., Hacker D.L., Wurm F.M. Valproic acid enhances recombinant mRNA and protein levels in transiently transfected Chinese hamster ovary cells. J Biotechnol 2010, 20(148(2-3)):128-132.
156. Wurm F.M. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol 2004, 22:1393-1398.
157. Xing Z., Li Z., Chow V., Lee S.S. Identifing inhibitory threshold values of repressing metabolites in CHO cell culture using multivariate analysis methods. Biotechnol Prog 2008, 24:675-683.
158. Yallop C., Crowley J., Cote J., Hegmans-Brouwer K., Lagerwerf F., Gagne F., et al. PER.C6 cells for the manufacture of biopharmaceutical proteins. Modern Biopharmaceuticals 2008, 779-807. K. Jorg (Ed.).
159. Ye J., Kober V., Tellers M., Naji Z., Salmon P., Markusen J.F. High-level protein expression in scalable CHO transient transfection. Biotechnol Bioeng 2009, 103:542-551.
160. Ye J., Alvin K., Latif H., Hsu A., Parikh V., Whitmer T., et al. Rapid protein production using CHO stable transfection pools. Biotechnol Prog 2010, 26:1431-1437.
161. Yoon S.K., Choi S.L., Song J.Y., Lee G.M. Effect of culture pH on erythropoietin production by Chinese hamster ovary cells grown in suspension at 32.5 and 37 degrees C. Biotechnol Bioeng 2005, 89:345-356.
162. Yoon S.K., Kima S.H., Song J.Y., Lee G.M. Biphasic culture strategy for enhancing volumetric erythropoietin productivity of Chinese hamster ovary cells. Enzyme Microb Technol 2006, 39:362-365.
163. Zhang J. Mammalian cell culture for biopharmaceutical production. Manual of Industrial Microbiology and Biotechnology 2010, 157-178. 3rd edition. R.H. Baltz (Ed.).
164. Zhang N., An Z. Heterologous protein expression in yeasts and filamentous fungi. Manual of Industrial Microbiology and Biotechnology 2010, 145-156. 3rd edition. R.H. Baltz (Ed.).
165. 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. Biotechnol Bioeng 2006, 95:1188-1197.
166. Zhang J., Liu X., Bell A., To R., Baral T.N., Azizi A., et al. Transient expression and purification of chimeric heavy chain antibodies. Protein Expr Purif 2009, 65:77-82.
167. Zhang F., Frost A.R., Blundell M.P., Bales O., Antoniou M.N., Thrasher A.J. A ubiquitous chromatin opening element (UCOE) confers resistance to DNA methylation-mediated silencing of lentiviral vectors. Mol Ther 2010, 18:1640-1649.
168. Zhao Y., Bishop B., Clay J.E., Lu W., Jones M., Daenke S., et al. Automation of large scale transient protein expression in mammalian cells. J Struct Biol. 2011, 175:209-215.
169. Zhou H., Lu Z.G., Sun Z.W., Yu W.Y. Development of site-specific integration system to high-level expression recombinant protein in CHO cells. Sheng Wu Gong Cheng Xue Bao (Chinese) 2007, 23:756-762.
170. Zhou H., Lu Z.G., Sun Z.W., Huang Y., Yu W.Y. Generation of stable cell lines by site-specific integration of transgenes into engineered Chinese hamster ovary strains using an FLP-FRT system. J Biotechnol 2010, 147:122-129.