Chapter 11 Selecting an Appropriate Method for Expressing a Recombinant Protein

Methods in Enzymology

Volumn 463, Issue C, 2009, Pages 131-147

  Brondyk, William H ^a  

^a GENZYME CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYTOPLASM PROTEIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; RECOMBINANT PROTEIN; SUMO PROTEIN; THIOREDOXIN;

BACULOVIRUS EXPRESSION SYSTEM; CODON USAGE; DISULFIDE BOND; ESCHERICHIA COLI; GENE EXPRESSION SYSTEM; HUMAN; INSECT CELL; MAMMAL CELL; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROCESSING; REVIEW; ANIMAL; BACULOVIRUS; DECISION MAKING; GENE EXPRESSION; GENE TRANSFER; GENETICS; GROWTH, DEVELOPMENT AND AGING; MAMMAL; METABOLISM; METHODOLOGY; PHYSIOLOGY; PICHIA;

ESCHERICHIA COLI; EUKARYOTA; MAMMALIA; PICHIA PASTORIS;

ANIMALS; BACULOVIRIDAE; CHOICE BEHAVIOR; ESCHERICHIA COLI; GENE EXPRESSION; GENE TRANSFER TECHNIQUES; HUMANS; MAMMALS; PICHIA; RECOMBINANT PROTEINS; RESEARCH DESIGN;

EID: 71549157111     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)63011-1     Document Type: Chapter

References (60)

1. Aguiar R.W., Martins E.S., Valicente F.H., Carneiro N.P., Batista A.C., Melatti V.M., Monnerat R.G., and Ribeiro B.M. A recombinant truncated Cry1Ca protein is toxic to lepidopteran insects and forms large cuboidal crystals in insect cells. Curr. Microbiol. 53 (2006) 287-292
2. Andersen C.L., Matthey-Dupraz A., Missiakas D., and Raina S. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol. Microbiol. 26 (1997) 121-132
3. Andersson D.I., Boham K., Isaksson L.A., and Kurland C.G. Translation rates and misreading characteristics of rpsD mutants in Escherichia coli. Mol. Gen. Genet. 187 (1982) 467-472
4. Baldi L., Hacker D.L., Adam M., and Wurm F.M. Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives. Biotechnol. Lett. 29 (2007) 677-684
5. Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
6. Bardwell J.C. Building bridges: Disulphide bond formation in the cell. Mol. Microbiol. 14 (1994) 199-205
7. Bessette P.H., Aslund F., Beckwith J., and Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96 (1999) 13703-13708
8. Bhatia P.K., and Mukhopadhyay A. Protein glycosylation: Implications for in vivo functions and therapeutic applications. Adv. Biochem. Eng. Biotechnol. 64 (1998) 155-201
9. Browne S.M., and Al-Rubeai M. Selection methods for high-producing mammalian cell lines. Trends Biotechnol. 25 (2007) 425-432
10. Butler M. Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems. Cytotechnology 50 (2006) 57-76
11. Celik E., Calik P., Halloran S.M., and Oliver S.G. Production of recombinant human erythropoietin from Pichia pastoris and its structural analysis. J. Appl. Microbiol. 103 (2007) 2084-2094
12. Chen W., Shen Q., and Bahl O.P. Carbohydrate variant of the recombinant β-subunit of human choriogonadotropin expressed in baculovirus expression system. J. Biol. Chem. 266 (1991) 4081-4087
13. Cregg J.M. Introduction: Distinctions between Pichia pastoris and other expression systems. Methods Mol. Biol. 389 (2007) 1-10
14. Cregg J.M., Barringer K.J., Hessler A.Y., and Madden K.R. Pichia pastoris as a host system for transformation. Mol. Cell. Biol. 5 (1985) 3376-3385
15. Daly R., and Hearn M.T.W. Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineering and production. J. Mol. Recognit. 18 (2005) 119-138
16. Dong M.S., Bell L.C., Guo Z., Phillips D.R., Blair I.A., and Guengerich F.P. Identification of retained N-formylmethionine in bacterial recombinant mammalian cytochrome P450 proteins with the N-terminal sequence MALLLAVFL...: Roles of residues 3-5 in retention and membrane topology. Biochemistry 35 (1996) 10031-10041
17. Durocher Y., Perret S., and Kamen A. High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30 (2002) E9
18. Dyson M.R., Shadbolt S.P., Vincent K.J., Perera R.L., and McCafferty J. Production of soluble mammalian proteins in Escherichia coli: Identification of protein features that correlate with successful expression. BMC Biotechnol. 4 (2004) 32-49
19. Esposito D., and Chatterjee D.K. Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 17 (2006) 353-358
20. Figueroa B., Ailor E., Osborne D., Hardwick J.M., Reff M., and Betenbaugh M.J. Enhanced cell culture performance using inducible anti-apoptotic genes E1B-19 K and Aven in the production of a monoclonal antibody with Chinese Hamster Ovary cells. Biotechnol. Bioeng. 97 (2007) 877-892
21. Gemmill T.R., and Trimble R.B. Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1426 (1999) 227-237
22. Giglione C., Boularot A., and Meinnel T. Review: Protein N-terminal methionine excision. Cell. Mol. Life Sci. 61 (2004) 1455-1474
23. Girard P., Derousazi M., Baumgartner G., Bourgeois M., Jordan M., Jacko B., and Wurm F.M. 100-liter transient transfection. Cytotechnology 38 (2002) 15-21
24. Gleeson M.A., White C.E., Meininger D.P., and Komives E.A. Generation of protease-deficient strains and their use in heterologous protein expression. Methods Mol. Biol. 103 (1998) 81-94
25. Goto M. Protein O-glycosylation in fungi: Diverse structures and multiple functions. Biosci. Biotechnol. Biochem. 71 (2007) 1415-1427
26. Goustin A.S., and Wilt F.H. Direct measurement of histone peptide elongation rate in cleaving sea urchin embryos. Biochim. Biophys. Acta 699 (1982) 22-27
27. Gustafsson C., Govindarajan S., and Minshull J. Codon bias and heterologous protein expression. Trends Biotechnol. 22 (2004) 346-353
28. Hamilton S.R., and Gerngross T.U. Glycosylation engineering in yeast: The advent of fully humanized yeast. Curr. Opin. Biotechnol. 18 (2007) 387-392
29. Harrison R.L., and Jarvis D.L. Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce "mammalianized" recombinant glycoproteins. Adv. Virus Res. 68 (2006) 159-191
30. Hitchman R.B., Siaterli E.A., Nixon C.P., and King L.A. Quantitative real-time PCR for rapid and accurate titration of recombinant baculovirus particles. Biotechnol. Bioeng. 96 (2007) 810-814
31. Ikonomou L., Schneider Y., and Agathos S.N. Insect cell culture for industrial production of recombinant proteins. Appl. Microbiol. Biotechnol. 62 (2003) 1-20
32. Jana S., and Deb J.K. Strategies for efficient production of heterologous proteins in Escherichia coli. Appl. Microbiol. Biotechnol. 67 (2005) 289-298
33. Jenkins N., Parekh R.B., and James D.C. Getting the glycosylation right: implications for the biotechnology industry. Nat. Biotechnol. 14 (1996) 975-981
34. Jordan M., Schallhorn A., and Wurm F.M. Transfecting mammalian cells: Optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res. 24 (1996) 596-601
35. Kane J.F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6 (1995) 494-500
36. Korth K.L., and Levings C.S. Baculovirus expression of the maize mitochondrial protein URF13 confers insecticidal activity in cell cultures and larvae. Proc. Natl. Acad. Sci. USA 90 (1993) 3388-3392
37. Kost T.A., Condreay J.P., and Jarvis D.L. Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol. 23 (2005) 567-575
38. Kwaks T.H.J., and Otte A.P. Employing epigenetics to augment the expression of therapeutic proteins in mammalian cells. Trends Biotechnol. 24 (2006) 137-142
39. Kwon M.S., Dojima T., Toriyama M., and Park E.Y. Development of an antibody-based assay for determination of baculovirus titers in 10 hours. Biotechnol. Prog. 18 (2002) 647-651
40. LaVallie E.R., DiBlasio E.A., Kovacic S., Grant K.L., Schendel P.F., and McCoy J.M. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Biotechnology (NY) 11 (1993) 187-193
41. Marin M. Folding at the rhythm of the rare codon beat. Biotechnol. J. 3 (2008) 1047-1057
42. Monsma S.A., and Scott M. BacVector-3000: An engineered baculovirus designed for greater protein stability. Innovations (1997) 16-19
43. Peter-Katalinic J. O-glycosylation of proteins. Methods Enzymol. 405 (2005) 139-171
44. Prasad S.V., Mujtaba S., Lee V.H., and Dunbar B.S. Immunogenicity enhancement of recombinant rabbit 55-kilodalton zona pellucida protein expressed using the baculovirus expression system. Biol. Reprod. 52 (1995) 1167-1178
45. Presta L.G. Molecular engineering and design of therapeutic antibodies. Curr. Opin. Immunol. 20 (2008) 460-470
46. Rossi F.M., and Blau H.M. Recent advances in inducible gene expression systems. Curr. Opin. Biotechnol. 9 (1998) 451-456
47. Sahdev S., Khattar S.K., and Saini K.S. Production of active eukaryotic proteins through bacterial expression systems: A review of existing biotechnology strategies. Mol. Cell Biochem. 307 (2008) 249-264
48. Saida F. Overview on the expression of toxic gene products in Escherichia coli. Curr. Protoc. Protein Sci. (2007) 5.19.1-5.19.13
49. Sarramegna V., Talmont F., Demange P., and Milon A. Heterologous expression of G-protein-coupled receptors: Comparison of expression systems from the standpoint of large-scale production and purification. Cell. Mol. Life Sci. 60 (2003) 1529-1546
50. Shinkawa T., Nakamura K., Yamane N., Shoji-Hosaka E., Kanda Y., Sakurada M., Uchida K., Anazawa H., Satoh M., Yamasaki M., Hanai N., and Shitara K. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 278 (2003) 3466-3473
51. Spiess C., Beil A., and Ehrmann M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 (1999) 339-347
52. Strausberg R.L., and Strausberg S.L. Overview of protein expression in Saccharomyces cerevisiae. Curr. Protoc. Protein Sci. (2001) Unit 5.6 Chapter 5
53. Sugyiama K., Ahorn H., Maurer-Fogy I., and Voss T. Expression of human interferon-α2 in Sf9 cells: Characterization of O-linked glycosylation and protein heterogeneities. Eur. J. Biochem. 217 (1993) 921-927
54. Thomsen D.R., Post L.E., and Elhammer A.P. Structure of O-glycosidically linked oligosaccharides synthesized by the insect cell line Sf9. J. Cell. Biochem. 43 (2004) 67-79
55. Trimble R.B., Lubowski C., Hauer C.R., Stack R., McNaughton L., Gemmill T.R., and Kumar S.A. Characterization of N- and O-linked glycosylation of recombinant human bile salt-stimulated lipase secreted by Pichia pastoris. Glycobiology 14 (2004) 265-274
56. Vera A., Gonzalez-Montalban N., Aris A., and Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol. Bioeng. 96 (2006) 1101-1106
57. Waugh D.S. Making the most of affinity tags. Trends Biotechnol. 23 (2005) 316-320
58. Weigel P.H., and Yik J.H.N. Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim. Biophys. Acta 1372 (2002) 341-363
59. Wurm F.M. Production of recombinant protein therapeutics in cultivated mammalian cells. Nature Biotechnol. 22 (2004) 1393-1398
60. Young J.C., Agashe V.R., Siegers K., and Hartl P.U. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5 (2004) 781-791