PERKEMBANGAN TEKNOLOGI SEL MAMALIA CHINESE HAMSTER OVARY (CHO) UNTUK PRODUKSI OBAT BERBASIS PROTEIN

Adi Santoso
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Abstract

Chinese hamsters ovary (CHO) and its derivative such as CHO-DXB11 cells, CHO-K1, CHO-DG44 and CHO-S are mammalian cells that are often used for production of therapeutic protein drugs. The CHO cells often used for protein production have several advantages including 1) host cells that are safe to use in drug production, 2) the level of production of proteins produced can be increased by amplifying genes using methotrexate (MTX), 3) having the capacity to make post-translation modificationsand 4) CHO cells can be adapted to grow in suspension. The high need for protein-based drugs triggers the development of basic knowledge and innovation in production of recombinant proteins. The impressive technological advances in CHO cell technology have made these cells can be used to produce proteins around 10 g/liter in order to meet the market demand. The first protein successfully produced using CHO mammalian cells was the therapeutic Tissue Plasminogen Activator (r-tPA, Activase) protein used for stroke patients. The presence of this drug is quickly followed by several other types of drugs. In this review, history of development of CHO cells, the contribution of CHO cells to basic research, progress of effective line cell screening and development technology are discussed.

Keywords

Chinese hamster ovary, CHO, therapeutic protein, mammalian cell

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Altamirano, C., Berrios, J., Vergara, M. and Becerra, S., 2013. Advances in improving mammalian cells metabolism for recombinant protein production, Electronic Journal of Biotechnology, 16(3), pp. 1-14.

Bailey, S.W and Ayling, J.E., 2009. The extremely slow and variable activity of dihydrofolate reductase in human liver and its implications for high folic acid intake. PNAS, 106 (36), pp. 15424–15429.

Batista, L.F., Chigancas, V., Brumatti, G., Amarante-Mendes, G.P. and Menck, C.F., 2006. Involvement of DNA replication in ultraviolet-induced apoptosis of mammalian cells. Apoptosis,11, pp. 1139-48.

Biedler, J.L. and Spengler, B.A., 1976. A novel chromosome abnormality in human neuroblastoma and antifolate resistant Chinese hamster cell lines in culture. J. Natl. Cancer Inst, 57, pp. 683–689.

Boeger, H., Bushnell, D.A., Davis, R., Griesenbeck, J., Lorch, Y., Strattan, J.S., Westover, K.D. and Kornberg, R.D., 2005. Structural basis of eukaryotic gene transcription. FEBS Lett, 579, pp. 899–903.

Cai, Y., Ludeman, S.M., Wilson, L.R., Chung, A.B. and Dolan, M.E., 2001. Effect of O6-benzylguanine on nitrogen mustard-induced toxicity, apoptosis, and mutagenicity in Chinese hamster ovary cells. Mol Cancer Ther, 1, pp. 21-28.

Calo, F.A.B. and Marto, A.H., 2012. Biosimilars: company strategies to capture value from the biologics market. Pharmaceuticals, 5, pp. 1393-408.

Chasin, L.A. and Urlaub, G., 1975. Chromosome-wide event accompanies the expression of recessive mutations in tetraploid cells. Science , 187, pp. 1091-1093.

Chen, MJ., Shimada, T., Moulton, A.D., Cline, A., Humphries, R.K., Maizel, J. and Nienhuis AW., 1984. The functional human dihydrofolate reductase gene. The Journal of Biological Chemistry, 259 (6), pp. 3933–3943.

Davies, S.L., Lovelady, C.S., Grainger, R.K., Racher, A.J., Young, R.J. and James, D.C., 2013. Functional heterogeneity and heritability in CHO cell populations. Biotechnol. Bioeng, 110, pp. 260–274.

Dietmair, S., Nielsen, L.K. and Timmins, N.E., 2011. Engineering a mammalian super producer. Journal of Chemical Technology and Biotechnology, 86(7), pp. 905-914.

Fernandez, M.J., Lopez, A. and Santa-Maria, A., 2003. Apoptosis induced by different doses of caffeine on Chinese hamster ovary cells. J Appl Toxicol. 23, pp. 221-224.

Florian, M.W., 2013. CHO Quasispecies: Implications for Manufacturing Processes. Processes,1, pp. 296-311.

Ghaderi, D., Zhang, M., Hurtado-Ziola, N. and Varki, A., 2012. Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation. Biotechnol. Genet. Eng. Rev, 28, pp. 147–175.

Gibco: User Manual – Freedomtm DG44 Kit 2011. Catalog no. A13737-01.

Gupta. S.K and Shukla, P., 2016. Advanced technologies for improved expression of recombinant proteins in bacteria: perspectives and applications. Crit Rev Biotechnol, 36, pp. 1089-1098.

Gupta, S.K. and Shukla, P., 2017. Microbial platform technology for recombinant antibody fragment production: A review. Crit Rev Microbiol, 43, pp. 31-42.

Gupta, S.K., Santosh, K.S., Ankit, S., Vaibhav, H.H., Nalagel, D.S., Hiralal, K., Nikhil, B.C. and Pratyoosh, S., 2017. Metabolic engineering of CHO cells for the development of a robust protein production platform. PLoS ONE, 12(8): e0181455.

Huang,Y.M., Hu, W., Rustandi, E., Chang, K., Yusuf, M.H. and Ryll, T., 2010. Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment. Biotechnol Prog, 26, pp. 1400-1410.

Jayapal, K.P., Wlaschin, K.F., Hu, W.S. and Yap M.G., 2007. Recombinant protein therapeutics from CHO cells-20 years and counting. Chem Eng Prog, 103, pp. 40–47.

Kaufman, R.J. and Schimke, R.T., 1981. Amplification and loss of dihydrofolate reductase genes in a Chinese hamster ovary cell line. Mol. Cell. Biol,12, pp. 1069–1076.

Kaufman, R.J. and Sharp, P.A., 1982. Amplification and expression of sequences cotransfected with a modular dihydrofolate reductase complementary dna gene. J. Mol. Biol. 159, pp. 601–621.

Kaufman, R.J., Wasley, L.C., Spiliotes, A.J., Gossels, S.D.,Latt, S.A., Larsen, G.R. and Kay, R. M., 1985. Coamplification and co-expression of human tissue-type plasminogen activator and murine dihydrofolate reductase sequences in Chinese Hamster Ovary cells. Mol. Cell. Biol, 5, pp. 1750–1759.

Kim, J.Y., Kim, Y.G. and Lee, G.M., 2012. CHO cells in biotechnology for production of recombinant proteins: current state and further potential. Appl Microbiol Biotechnol, 93, pp. 917–930

Lai,T., Yang, Y. and Kong, S. 2013. Advances in Mammalian Cell Line Development Technologies for Recombinant Protein Production. Pharmaceuticals, 6, pp. 579-603.

Lim, Y., Wong, N.S.C., Lee, Y.L., Ku, S.C.Y., Wong, D.C.F. and Yap, M.G.S., 2010. Engineering mammalian cells in bioprocessing-current achievements and future perspectives. Biotechnology Applied Biochemistry, 55(4), pp. 175-189.

Omasa, T., Onitsuka, M. and Kim, W.D., 2010. Cell engineering and cultivation of Chinese hamster ovary (CHO) cells. Current Pharmaceutical Biotechnology, 11(3), pp. 233-240.

Pallavicini, M.G., DeTeresa, P.S., Rosette, C., Gray, J.W. and Wurm, F.M., 1990. Effects of Methotrexate (MTX) on Transfected DNA Stability in Mammalian Cells. Mol. Cell. Biol, 10, pp. 401–404.

Puck, T.T., 1957. The genetics of somatic mammalian cells. Adv. Biology. Med. Physics, 5, pp. 75–101.

Puck, T.T., 1985. Development of the Chinese Hamster Ovary (CHO) Cell for Use in Somatic Cell Genetics. In Molecular Cell Genetics; Gottesman, M.M., ed.; John Wiley and Sons: New York, NY, USA, pp. 37–64.

Puck, T.T. and Kao, F.T., 1967. Genetics of somatic mammalian cells. V. Treatment with 5-bromodeoxyuridine and visible light for isolation of nutritionally deficient mutants. PNAS, 58, pp. 1227-1234.

Reinhart, D., Damjanovic, L., Kaisermayer, C., Sommeregger, W., Gili, A., Gasselhuber, B., Castan, A., Mayrhofer, P., Grünwald-Gruber, C. and Kunert R., 2018. Bioprocessing of Recombinant CHO-K1, CHO-DG44, and CHO-S: CHO Expression Hosts Favor Either mAb Production or Biomass Synthesis. Biotechnol J, 1700686, pp. 1-11

Schmidt, F.L., Leslie, L.G,, Schultz, J.R. and Gerritsen GC., 1970. Epidemiological studies of the Chinese hamster. Diabetologia. 6(3), pp. 154-7.

Schroder, M., 2008. Engineering eukaryotic protein factories. Biotechnology Letters, 30(2), pp. 187-196.

Soloneski, S., Gonzalez, M., Piaggio, E., Reigosa, M.A. and Larramendy, M.L., 2002. Effect of dithiocarbamate pesticide zineb and its commercial formulation, azzurro. III. Genotoxic evaluation on Chinese hamster ovary (CHO) cells. Mutat Res, 15, pp. 201-212.

Sommeregger, W., Gili, A., Sterovsky, T., Casanova, E. and Kunert, R., 2013. Powerful expression in Chinese Hamster Ovary cells using bacterial artificial chromosomes: Parameters influencing productivity. BMC Proceedings, 7(S6), P2.

Sunley, K. and Butler, M., 2010. Strategies for the enhancement of recombinant protein production from mammalian cells by growth arrest. Biotechnology Advances, 28(3), pp. 385-394.

Urlaub, G. and Chasin, L.A., 1980. Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity. PNAS, 77 (7), pp. 4216–4220.

Urlaub, G., Kas, E., Carothers, A.M. and Chasin, L.A., 1983. Deletion of the diploid dihydrofolate reductase locus form cultured mammalian cells. Cell, 33, pp. 405–412.

Urlaub, G., Mitchell, P.J., Kas, E., Chasin, L.A., Fumanage, V.L., Myoda, T.T. and Hamlin, J., 1986. Effect of gamma rays at the dihydrofolate reductase locus: Deletions and inversions. Somat. Cell Mol.Genet, 12, pp. 555–566.

Walsh, G., 2014. Biopharmaceutical benchmarks. Nat Biotechnol, 32, pp. 992-1000.

Walsh, C.T., Garneau-Tsodikova, J. and Gatto JR., 2005. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed Engl, 44(45), pp. 7342-72.

Weerapana, E. and Imperiali, B., 2006. Asparagine-linked protein glycosylation: from

eukaryotic to prokaryotic systems. Glycobiology, 16(6), pp 91R–101R.

Weidle, U.H., Buckel, P. and Wienberg, J., 1988. Amplified expression constructs for human tissue type plasminogen activator in CHO cells: Instability in the absence of selective pressure. Gene, 66, pp. 193–203.

Wiberg, F.C., Rasmussen, S.K., Frandsen, T.P., Rasmussen, L.K., Tengbjerg, K., Coljee, V.W., Sharon, J., Yang, C.Y., Bregenholt, S., Nielsen, L.S., 2006. Production of target-specific recombinant human polyclonal antibodies in mammalian cells. Biotechnol. Bioeng, 94, pp. 396–405.

Wurm, F.M., 1990. Integration, amplification and stability of plasmid sequences in CHO cell cultures. Biologicals, 18, pp. 159–164.

Wurm, F.M., 2004. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol, 22, pp. 1393–1398.

Wurtele, H., Little, K.C. and Chartrand, P., 2003. Illegitimate DNA integration in mammalian cells. Gene Ther, 10, pp. 1791–1799.

Xu, J., Ge, X. and Dolan, M.C., 2011. Towards high-yield production of pharmaceutical proteins with plant cell suspension cultures. Biotechnol Adv, 29, pp. 278-299.

Zhu, J., 2012. Mammalian cell protein expression for biopharmaceutical production. Biotechnol Adv, 30, pp. 1158-1170.


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