Application of destabilizing sequences on selection marker for improved recombinant protein productivity in CHO-DG44

Metabolic Engineering

Volumn 9, Issue 3, 2007, Pages 304-316

  Ng, Say Kong ^a   Wang, Daniel I C ^a,b   Yap, Miranda G S ^a,c  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b Massachusetts Institute of Technology Cambridge   (United States)

^c AGENCY FOR SCIENCE   (Singapore)

Author keywords

AU rich elements; CHO DG44; Dihydrofolate reductase; Interferon gamma; Mammalian cell culture; Methotrexate amplification; Murine ornithine decarboxylase; PEST region; Recombinant protein expression

Indexed keywords

BIOCOMPATIBILITY; BIOMARKERS; CELL CULTURE; ENZYME KINETICS; GENE EXPRESSION;

DIHYDROFOLATE REDUCTASE; MAMMALIAN CELL CULTURE; METHOTREXATE AMPLIFICATION; MURINE ORNITHINE DECARBOXYLASE; RECOMBINANT PROTEIN EXPRESSION;

PROTEINS;

DIHYDROFOLATE REDUCTASE; GAMMA INTERFERON; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D; MESSENGER RNA; METHOTREXATE; MOLECULAR MARKER; ORNITHINE DECARBOXYLASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CHO CELL; CONTROLLED STUDY; EXPRESSION VECTOR; GENE AMPLIFICATION; GENETIC TRANSFECTION; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STABILITY; RAT; SEQUENCE CHARACTERIZED AMPLIFIED REGION;

3' UNTRANSLATED REGIONS; ANIMALS; CHO CELLS; CRICETINAE; CRICETULUS; GENETIC MARKERS; GENETIC VECTORS; HUMANS; INTERFERON TYPE II; MICE; RECOMBINANT PROTEINS; RNA STABILITY; TETRAHYDROFOLATE DEHYDROGENASE;

MAMMALIA; MURINAE;

EID: 34249741495     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2007.01.001     Document Type: Article

References (39)

1. Bakheet T., Frevel M., Williams B.R.G., Greer W., and Khabar K.S.A. ARED: human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins. Nucl. Acids Res. 29 1 (2001) 246-254
2. Bakheet T., Williams B.R.G., and Khabar K.S.A. ARED 2.0: an update of AU-rich element mRNA database. Nucl. Acids Res. 31 1 (2003) 421-423
3. Butler M. Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals. Appl. Microbiol. Biotechnol. 68 (2005) 283-291
4. Chen L., Xie Z., Teng Y., Wang M., Shi M., Qian L., Hu M., Feng J., Yang X., Shen B., and Guo N. Highly efficient selection of the stable clones expressing antibody-IL-2 fusion protein by a dicistronic expression vector containing a mutant neo gene. J. Immunol. Methods 295 (2004) 49-56
5. Corish P., and Tyler-Smith C. Attenuation of green fluorescent protein half-life in mammalian cells. Prot. Eng. 12 12 (1999) 1035-1040
6. Flintoff W.F., Davidson S.V., and Siminovitch L. Isolation and partial characterization of three methotrexate-resistant phenotypes from Chinese hamster ovary cells. Somat. Cell Genet. 2 3 (1976) 245-261
7. Fox S.R., Patel U.A., Yap M.G.S., and Wang D.I.C. Maximizing Interferon-γ production by Chinese hamster ovary cells through temperature shift optimization: experimental and modeling. Biotechnol. Bioeng. 85 2 (2004) 177-184
8. Fox S.R., Tan H.K., Tan M.C., Wong S.C.N., Yap M.G.S., and Wang D.I.C. Detailed understanding of the enhanced hypothermic productivity of interferon-γ by Chinese hamster ovary cells. Biotechnol. Appl. Biochem. 41 (2005) 255-264
9. Ghoda L., van Daalen Wetters T., Macrae M., Ascherman D., and Coffino P. Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation. Science 243 (1989) 1493-1495
10. Ghoda L., Sidney D., Macrae M., and Coffino P. Structural elements of ornithine decarboxylase required for intracellular degradation and polyamine-dependent regulation. Mol. Cell. Biol. 12 5 (1992) 2178-2185
11. Gilon T., Chomsky O., and Kulka R.G. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J. 17 (1998) 2759-2766
12. Goldman M.H., James D.C., Rendall M., Ison A.P., Hoare M., and Bull A.T. Monitoring recombinant human interferon-gamma N-glycosylation during perfused fluidized-bed and stirred-tank batch culture of CHO cells. Biotechnol. Bioeng. 60 5 (1998) 596-607
13. Gross G., and Hauser H. Heterologous expression as a tool for gene identification and analysis. J. Biotechnol. 41 (1995) 91-110
14. Guhaniyogi J., and Brewer G. Regulation of mRNA stability in mammalian cells. Gene 265 1-2 (2001) 11-23
15. Haber D.A., Beverley S.M., Kiely M.L., and Schimke R.T. Properties of an altered dihydrofolate reductase encoded by amplified genes in cultured mouse fibroblasts. J. Biol. Chem. 256 (1981) 9501-9510
16. Hayter P.M., Curling E.M.A., Baines A.J., Jenkins N., Salmon I., Strange P.G., and Bull A.T. Chinese hamster ovary cell growth and interferon production kinetics in stirred batch culture. Appl. Microbiol. Biotechnol. 34 (1991) 559-564
17. Kaufman R.J., and Sharp P.A. Amplification and expression of sequences cotransfected with a modular dihydrofolate reductase cDNA gene. J. Mol. Biol. 159 (1982) 601-621
18. Kim N.S., Byun T.H., and Lee G.M. Key determinants in the occurrence of clonal variation in humanized antibody expression of CHO cells during dihydrofolate reductase mediated gene amplification. Biotechnol. Prog. 17 (2001) 69-75
19. Lamotte D., Buckberry L., Monaco L., Soria M., Jenkins N., Engasser J.M., and Marc A. Na-butyrate increases the production and α2,6-sialylation of recombinant interferon-γ expressed by α2,6-sialyltransferase engineered CHO cells. Cytotechnology 29 (1999) 55-64
20. Laney J.D., and Hochstrasser M. Substrate targeting in the ubiquitin system. Cell 97 (1999) 427-430
21. Li X., Zhao X., Fang Y., Jiang X., Duong T., Fan C., Huang C.C., and Kain S.R. Generation of destabilized green fluorescent protein as a transcription reporter. J. Biol. Chem. 273 52 (1998) 34970-34975
22. -ΔΔCt method. Methods 25 (2001) 402-408
23. Loetscher P., Pratt G., and Rechsteiner M. The C terminus of mouse ornithine decarboxylase confers rapid degradation on dihydrofolate reductase. J. Biol. Chem. 266 15 (1991) 11213-11220
24. Niwa H., Yamamura K., and Miyazaki J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108 (1991) 193-200
25. Ririe K.M., Rasmussen R.P., and Wittwer C.T. Product differentiation by analysis of DNA melting curves during the polymerase chain reaction. Anal. Biochem. 245 (1997) 154-160
26. Rogers S., Wells R., and Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234 (1986) 364-368
27. Ross J. mRNA stability in mammalian cells. Microbiol. Rev. 59 3 (1995) 423-450
28. Sautter K., and Enenkel B. Selection of high-producing CHO cells using NPT selection marker with reduced enzyme activity. Biotechnol. Bioeng. 89 5 (2005) 530-538
29. Scahill S.J., Devos J., Van der Heyden J., and Fiers W. Expression and characterization of the product of a human immune interferon cDNA gene in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 80 (1983) 4654-4658
30. Suzuki T., and Varshavsky A. Degradation signals in the lysine-asparagine sequence space. EMBO J. 18 21 (1999) 6017-6026
31. Urlaub G., Kas E., Carothers A.M., and Chasin L.A. Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells. Cell 33 (1983) 405-412
32. Varshavsky A. The N-end rule. Cell 69 5 (1992) 725-735
33. Voon D.C., Subrata L.S., Baltic S., Leu M.P., Whiteway J.M., Wong A., Knight S.A., Christiansen F.T., and Daly J.M. Use of mRNA- and protein-destabilizing elements to develop a highly responsive reporter system. Nucl. Acids Res. 33 3 (2005) e27
34. Wong D.C.F., Wong K.T.K., Goh L.T., Heng C.K., and Yap M.G.S. Impact of dynamic online fed-batch strategies on metabolism, productivity and N-glycosylation quality in CHO cell cultures. Biotechnol. Bioeng. 89 2 (2005) 164-177
35. Wurm F.M. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol. 22 (2004) 1393-1398
36. Xie L., Nyberg G., Gu X., Li H., Mollborn F., and Wang D.I.C. Gamma-interferon production and quality in stoichiometric fed-batch cultures of Chinese hamster ovary (CHO) cells under serum-free conditions. Biotechnol. Bioeng. 56 5 (1997) 577-582
37. Zdanovsky, A., Zdanovskaia, M., Ma, D., Wood, K.V., Almond, B., Wood, M.G., 2004. Rapidly degraded reporter fusion proteins. United States Patent US2004/0146987 A1.
38. Zhang M., MacDonald A.I., Hoyt M.A., and Coffino P. Proteasomes begin ornithine decarboxylase digestion at the C terminus. J. Biol. Chem. 279 20 (2004) 20959-20965
39. Zubiaga A.M., Belasco J.G., and Greenberg M.E. The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation. Mol. Cell. Biol. 15 4 (1995) 2219-2230