Heterologous protein production using euchromatin-containing expression vectors in mammalian cells

Nucleic Acids Research

Volumn 43, Issue 16, 2015, Pages

  Zboray, Katalin ^a   Sommeregger, Wolfgang ^b,c   Bogner, Edith ^a   Gili, Andreas ^c   Sterovsky, Thomas ^c   Fauland, Katharina ^c   Grabner, Beatrice ^a   Stiedl, Patricia ^a   Moll, Herwig P ^d   Bauer, Anton ^e   Kunert, Renate ^b   Casanova, Emilio ^a,d  

^a MEDICAL UNIVERSITY OF VIENNA   (Austria)

^b UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^c Polymun Scientific GmbH   (Austria)

^d MEDICAL UNIVERSITY OF VIENNA   (Austria)

^e Antibody Lab   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; GLYCOPROTEIN GP 140; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY; RECOMBINANT PROTEIN; EUCHROMATIN; GLYCOPROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; IMMUNOGLOBULIN FC FRAGMENT;

ANIMAL CELL; ARTICLE; BACTERIAL ARTIFICIAL CHROMOSOME; BIOREACTOR; CHO CELL LINE; CHROMATIN; CONTROLLED STUDY; EUCHROMATIN; EXPRESSION VECTOR; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN EXPRESSION; ANIMAL; BIOSYNTHESIS; CRICETULUS; GENE VECTOR; GENETICS; HAMSTER; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOLOGY;

ANIMALS; ANTIBODIES, NEUTRALIZING; CHO CELLS; CHROMOSOMES, ARTIFICIAL, BACTERIAL; CRICETINAE; CRICETULUS; EUCHROMATIN; GENETIC VECTORS; GLYCOPROTEINS; HIV ANTIBODIES; HIV-1; HUMAN IMMUNODEFICIENCY VIRUS PROTEINS; HUMANS; IMMUNOGLOBULIN FC FRAGMENTS; RECOMBINANT PROTEINS;

EID: 84942237261     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv475     Document Type: Article

References (51)

1. Zhu, J. (2012) Mammalian cell protein expression for biopharmaceutical production. Biotechnol. Adv., 30, 1158-1170.
2. Walsh, G. (2014) Biopharmaceutical benchmarks 2014. Nat. Biotechnol., 32, 992-1000.
3. Baldi, L., Hacker, D.L., Adam, M. and Wurm, F.M. (2007) Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives. Biotechnol. Lett., 29, 677-684.
4. Wurm, F. and Bernard, A. (1999) Large-scale transient expression in mammalian cells for recombinant protein production. Curr. Opin. Biotechnol., 10, 156-159.
5. Geisse, S. and Fux, C. (2009) Recombinant protein production by transient gene transfer into Mammalian cells. Methods Enzymol., 463, 223-238.
6. Hacker, D.L., De Jesus, M. and Wurm, F.M. (2009) 25 years of recombinant proteins from reactor-grown cells - where do we go from here? Biotechnol. Adv., 27, 1023-1027.
7. Xu, X., Nagarajan, H., Lewis, N.E., Pan, S., Cai, Z., Liu, X., Chen, W., Xie, M., Wang, W., Hammond, S. et al. (2011) The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line. Nat. Biotechnol., 29, 735-741.
8. Kildegaard, H.F., Baycin-Hizal, D., Lewis, N.E. and Betenbaugh, M.J. (2013) The emerging CHO systems biology era: harnessing the 'omics revolution for biotechnology. Curr. Opin. Biotechnol., 24, 1102-1107.
9. Datta, P., Linhardt, R.J. and Sharfstein, S.T. (2013) An 'omics approach towards CHO cell engineering. Biotechnol. Bioeng., 110, 1255-1271.
10. Dietmair, S., Nielsen, L.K. and Timmins, N.E. (2012) Mammalian cells as biopharmaceutical production hosts in the age of omics. Biotechnol. J., 7, 75-89.
11. 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, 917-930.
12. Wilson, C., Bellen, H.J. and Walter, G. (1990) Position effects on eukaryotic gene expression. Annu. Rev. Cell Biol, 6, 679-714.
13. Bandaranayake, A.D. and Almo, S.C. (2014) Recent advances in mammalian protein production. FEBS Lett., 588, 253-260.
14. Wurm, F.M. (2004) Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol., 22, 1393-1398.
15. Jun, S.C., Kim, M.S., Hong, H.J. and Lee, G.M. (2006) Limitations to the development of humanized antibody producing Chinese hamster ovary cells using glutamine synthetase-mediated gene amplification. Biotechnol. Prog., 22, 770-780.
16. Antoniou, M., Harland, L., Mustoe, T., Williams, S., Holdstock, J., Yague, E., Mulcahy, T., Griffiths, M., Edwards, S., Ioannou, P.A. et al. (2003) Transgenes encompassing dual-promoter CpG islands from the human TBP and HNRPA2B1 loci are resistant to heterochromatin-mediated silencing. Genomics, 82, 269-279.
17. Benton, T., Chen, T., McEntee, M., Fox, B., King, D., Crombie, R., Thomas, T.C. and Bebbington, C. (2002) 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, 38, 43-46.
18. Ye, J., Alvin, K., Latif, H., Hsu, A., Parikh, V., Whitmer, T., Tellers, M., de la Cruz Edmonds, M.C., Ly, J., Salmon, P. et al. (2010) Rapid protein production using CHO stable transfection pools. Biotechnol. Prog., 26, 1431-1437.
19. Zahn-Zabal, M., Kobr, M., Girod, P.-A., Imhof, M., Chatellard, P., de Jesus, M., Wurm, F. and Mermod, N. (2001) Development of stable cell lines for production or regulated expression using matrix attachment regions. J. Biotechnol., 87, 29-42.
20. Girod, P., Nguyen, D., Calabrese, D., Puttini, S., Martinet, D., Regamey, A., Saugy, D., Beckmann, J.S., Bucher, P. and Mermod, N. (2007) Genome-wide prediction of matrix attachment regions that increase gene expression in mammalian cells. Nat. Methods, 4, 747-753.
21. Kwaks, T.H.J., Barnett, P., Hemrika, W., Siersma, T., Sewalt, R.G. a B., Satijn, D.P.E., Brons, J.F., van Blokland, R., Kwakman, P., Kruckeberg, A.L. et al. (2003) Identification of anti-repressor elements that confer high and stable protein production in mammalian cells. Nat. Biotechnol., 21, 553-558.
22. Wirth, D., Gama-Norton, L., Riemer, P., Sandhu, U., Schucht, R. and Hauser, H. (2007) Road to precision: recombinase-based targeting technologies for genome engineering. Curr. Opin. Biotechnol., 18, 411-419.
23. Crawford, Y., Zhou, M., Hu, Z., Joly, J., Snedecor, B., Shen, A. and Gao, A. (2013) Fast identification of reliable hosts for targeted cell line development from a limited-genome screening using combined φC31 integrase and CRE-Lox technologies. Biotechnol. Prog., 29, 1307-1315.
24. Marshall, V.M., Allison, J., Templeton, T. and Foote, S.J. (2004) Generation of BAC transgenic mice. Methods Mol. Biol., 256, 159-182.
25. Van Keuren, M.L., Gavrilina, G.B., Filipiak, W.E., Zeidler, M.G. and Saunders, T.L. (2009) Generating transgenic mice from bacterial artificial chromosomes: transgenesis efficiency, integration and expression outcomes. Transgenic Res., 18, 769-785.
26. Yang, X.W. and Gong, S. (2005) An overview on the generation of BAC transgenic mice for neuroscience research. Curr. Protoc. Neurosci., Chapter 5, Unit 5.20.
27. Muyrers, J.P.P., Zhang, Y., Testa, G. and Stewart, A.F. (1999) Rapid modification of bacterial artificial chromosomes by ET-recombination. Nucleic Acids Res., 27, 1555-1557.
28. Zhang, Y., Buchholz, F., Muyrers, J.P. and Stewart, A.F. (1998) A new logic for DNA engineering using recombination in Escherichia coli. Nat. Genet., 20, 123-128.
29. Livak, K.J. and Schmittgen, T.D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods, 25, 402-408.
30. Soriano, P. (1999) Generalized lacZ expression with the ROSA26 Cre reporter strain. Nat. Genet., 21, 70-71.
31. Zambrowicz, B.P., Imamoto, A., Fiering, S., Herzenberg, L.A., Kerr, W.G. and Soriano, P. (1997) Disruption of overlapping transcripts in the ROSA beta geo 26 gene trap strain leads to widespread expression of beta-galactosidase in mouse embryos and hematopoietic cells. Proc. Natl. Acad. Sci. U.S.A., 94, 3789-3794.
32. Bronson, S.K., Plaehn, E.G., Kluckman, K.D. and Maeda, N. (1996) Single-copy transgenic mice with chosen-site integration. Proc. Natl. Acad. Sci. U.S.A., 93, 9067-9072.
33. Hatada, S., Kuziel, W., Smithies, O. and Maeda, N. (1999) The influence of chromosomal location on the expression of two transgenes in mice. J. Biol. Chem., 274, 948-955.
34. Urlaub, G. and Chasin, L.A. (1980) Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity. Proc. Natl. Acad. Sci. U.S.A., 77, 4216-4220.
35. Wirth, M., Bode, J., Zettlmeissl, G. and Hauser, H. (1988) Isolation of overproducing recombinant mammalian cell lines by a fast and simple selection procedure. Gene, 73, 419-426.
36. Chusainow, J., Yang, Y.S., Yeo, J.H.M., Toh, P.C., Asvadi, P., Wong, N.S.C. and Yap, M.G.S. (2009) A study of monoclonal antibody-producing CHO cell lines: what makes a stable high producer? Biotechnol. Bioeng., 102, 1182-1196.
37. Su, L., Graf, M., Zhang, Y., Von Briesen, H., Xing, H., Köstler, J., Melzl, H. and Wolf, H. (2000) Characterization of a virtually full-length human immunodeficiency virus type 1 genome of a prevalent intersubtype (C/B') recombinant strain in china characterization of a virtually full-length human immunodeficiency virus type 1 genome of a prevalen. J. Virol., 74, 11367-11376.
38. Pabst, M., Chang, M., Stadlmann, J. and Altmann, F. (2012) Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140. Biol. Chem., 393, 719-30.
39. Jeffs, S.A., Goriup, S., Kebble, B., Crane, D., Bolgiano, B., Sattentau, Q., Jones, S. and Holmes, H. (2004) Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1. Vaccine, 22, 1032-1046.
40. Zhang, C.W., Chishti, Y., Hussey, R.E. and Reinherz, E.L. (2001) Expression, purification, and characterization of recombinant HIV gp140. The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer. J. Biol. Chem., 276, 39577-39585.
41. McLellan, J.S., Pancera, M., Carrico, C., Gorman, J., Julien, J.-P., Khayat, R., Louder, R., Pejchal, R., Sastry, M., Dai, K. et al. (2011) Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature, 480, 336-343.
42. Nehlsen, K., Schucht, R., da Gama-Norton, L., Krömer, W., Baer, A., Cayli, A., Hauser, H. and Wirth, D. (2009) Recombinant protein expression by targeting pre-selected chromosomal loci. BMC Biotechnol., 9, 100.
43. Qin, J.Y., Zhang, L., Clift, K.L., Hulur, I., Xiang, A.P., Ren, B.-Z. and Lahn, B.T. (2010) Systematic comparison of constitutive promoters and the doxycycline-inducible promoter. PLoS One, 5, e10611.
44. Blaas, L., Musteanu, M., Eferl, R., Bauer, A. and Casanova, E. (2009) Bacterial artificial chromosomes improve recombinant protein production in mammalian cells. BMC Biotechnol., 9, 3.
45. Mader, A., Prewein, B., Zboray, K., Casanova, E. and Kunert, R. (2013) Exploration of BAC versus plasmid expression vectors in recombinant CHO cells. Appl. Microbiol. Biotechnol., 97, 4049-4054.
46. Eszterhas, S.K., Bouhassira, E.E., Martin, D.I.K. and Fiering, S. (2002) Transcriptional interference by independently regulated genes occurs in any relative arrangement of the genes and is influenced by chromosomal integration position. Mol. Cell. Biol., 22, 469-479.
47. Schlatter, S., Stansfield, S., Dinnis, D., Racher, A., Birch, J. and James, D. (2005) On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells. Biotechnol. Prog., 21, 122-133.
48. Dreesen, I.A.J. and Fussenegger, M. (2011) Ectopic expression of human mTOR increases viability, robustness, cell size, proliferation, and antibody production of chinese hamster ovary cells. Biotechnol. Bioeng., 108, 853-866.
49. Ku, S.C.Y., Ng, D.T.W., Yap, M.G.S. and Chao, S.-H. (2008) Effects of overexpression of X-box binding protein 1 on recombinant protein production in Chinese hamster ovary and NS0 myeloma cells. Biotechnol. Bioeng., 99, 155-164.
50. Cao, Y., Kimura, S., Itoi, T., Honda, K., Ohtake, H. and Omasa, T. (2012) Construction of BAC-based physical map and analysis of chromosome rearrangement in Chinese hamster ovary cell lines. Biotechnol. Bioeng., 109, 1357-1367.
51. Cong, L., Ran, F.A., Cox, D., Lin, S., Barretto, R., Habib, N., Hsu, P.D., Wu, X., Jiang, W., Marraffini, L.A. et al. (2013) Multiplex genome engineering using CRISPR/Cas systems. Science, 339, 819-123.