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Reliable protein production in a Pseudomonas fluorescens expression system

Retallack, Diane M., Jin, Hongfan, Chew, Lawrence·2012·Protein Expression and Purification
DOI 10.1016/j.pep.2011.09.010
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Abstract

A bottleneck to product development can be reliable expression of active target protein. A wide array of recombinant proteins in development, including an ever growing number of non-natural proteins, is being expressed in a variety of expression systems. A Pseudomonas fluorescens expression platform has been developed specifically for recombinant protein production. The development of an integrated molecular toolbox of expression elements and host strains, along with automation of strain screening is described. Examples of strain screening and scale-up experiments show rapid development of expression strains producing a wide variety of proteins in a soluble active form.

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Research works printed but not linked: 69

  1. Hacker, 2009, 25 years of recombinant proteins from reactor-grown cells - where do we go from here?, Biotechnol. Adv., 27, 1023, 10.1016/j.biotechadv.2009.05.008 · DOI
  2. Lim, 2010, Process economic benefits of expression technology based on Pseudomonas fluorescens, BioProcess Int., 8, 62
  3. Landry, 2003, Safety evaluation of an alpha-amylase enzyme preparation derived from the archaeal order Thermococcales as expressed in Pseudomonas fluorescens biovar I, Regul. Toxicol. Pharmacol., 37, 149, 10.1016/S0273-2300(03)00002-3 · DOI
  4. Silby, 2009, Genomic and genetic analyses of diversity and plant interactions of Pseudomonas fluorescens, Genome Biol., 10, R51, 10.1186/gb-2009-10-5-r51 · DOI
  5. Loper, 2007, The genomic sequence of Pseudomonas fluorescens Pf-5: insights into biological control, Phytopathology, 97, 233, 10.1094/PHYTO-97-2-0233 · DOI
  6. Paulsen, 2005, Complete genome sequence of the plant commensal Pseudomonas fluorescens Pf-5, Nat. Biotech., 23, 873, 10.1038/nbt1110 · DOI
  7. Scholz, 1989, Complete nucleotide sequence and gene organization of the broad-host-range plasmid RSF1010, Gene, 75, 271, 10.1016/0378-1119(89)90273-4 · DOI
  8. Nieto, 1990, Cloning vectors, derived from a naturally occurring plasmid of Pseudomonas savastanoi, specifically tailored for genetic manipulations in Pseudomonas, Gene, 87, 145, 10.1016/0378-1119(90)90507-N · DOI
  9. Artiguenave, 1997, High-efficiency transposon mutagenesis by electroporation of a Pseudomonas fluorescens strain, FEMS Microbiol. Lett., 153, 363, 10.1111/j.1574-6968.1997.tb12597.x · DOI
  10. Itoh, 1994, Efficient transformation of pseudomonas strains with pNI vectors by electroporation, Biosci. Biotechnol. Biochem., 58, 1306, 10.1271/bbb.58.1306 · DOI
  11. Maestro, 2003, Modulation of pPS10 Host Range by Plasmid-Encoded RepA Initiator Protein, J. Bacteriol., 185, 1367, 10.1128/JB.185.4.1367-1375.2003 · DOI
  12. Schneider, 2005, Auxotrophic markers pyrF and proC can replace antibiotic markers on protein production plasmids in high-cell-density Pseudomonas fluorescens fermentation, Biotechnol. Prog., 21, 343, 10.1021/bp049696g · DOI
  13. Alani, 1987, A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains, Genetics, 116, 541, 10.1093/genetics/116.4.541 · DOI
  14. Galvao, 2005, V. de Lorenzo, Adaptation of the yeast URA3 selection system to gram-negative bacteria and generation of a ΔbetCDE Pseudomonas putida strain, Appl. Environ. Microbiol., 71, 883, 10.1128/AEM.71.2.883-892.2005 · DOI
  15. Kwon-Chung, 1992, Selection of ura5 and ura3 mutants from the two varieties of Cryptococcus neoformans on 5-fluoroorotic acid medium, J. Med. Vet. Mycol., 30, 61, 10.1080/02681219280000081 · DOI
  16. Millerioux, 2011, Development of a URA5 integrative cassette for gene disruption in the Candida guilliermondii ATCC 6260 strain, J. Microbiol. Methods, 84, 355, 10.1016/j.mimet.2010.12.013 · DOI
  17. Romanos, 1991, Direct selection of stabilised yeast URA3 transformants with 5-fluorouracil, Nucleic Acids Res., 19, 187, 10.1093/nar/19.1.187 · DOI
  18. Woods, 1998, Rare homologous gene targeting in Histoplasma capsulatum: disruption of the URA5Hc gene by allelic replacement, J. Bacteriol., 180, 5135, 10.1128/JB.180.19.5135-5143.1998 · DOI
  19. Bagdasarian, 1983, Activity of the hybrid trp-lac (tac) promoter of Escherichia coli in Pseudomonas putida. Construction of broad-host-range, controlled-expression vectors, Gene, 26, 273, 10.1016/0378-1119(83)90197-X · DOI
  20. Ghosh, 1991, Specificity of antitermination mechanisms. Suppression of the terminator cluster T1–T2 of Escherichia coli ribosomal RNA operon, rrnB, by phage lambda antiterminators, J. Mol. Biol., 222, 59, 10.1016/0022-2836(91)90737-Q · DOI
  21. Hartmann, 1985, Expression of plasmid encoded Escherichia coli 5S ribosomal ribonucleic acid in Pseudomonas putida, FEBS Lett., 188, 295, 10.1016/0014-5793(85)80390-2 · DOI
  22. Calos, 1981, The DNA sequence change resulting from the IQ1 mutation, which greatly increases promoter strength, Mol. Gen. Genet., 183, 559, 10.1007/BF00268783 · DOI
  23. Simons, 1984, Possible ideal lac operator: Escherichia coli lac operator-like sequences from eukaryotic genomes lack the central G X C pair, Proc. Natl. Acad. Sci., 81, 1624, 10.1073/pnas.81.6.1624 · DOI
  24. Retallack, 2006, Identification of anthranilate and benzoate metabolic operons of Pseudomonas fluorescens and functional characterization of their promoter regions, Microb. Cell Fact., 5, 1, 10.1186/1475-2859-5-1 · DOI
  25. Yang, 2000, The effect of over-expression of chaperones on the secretion and the solubility of proteins, Zhongguo Shengwu Huaxue Yu Fenzi Shengwu Xuebao, 16, 382
  26. Barrick, 1994, Quantitative analysis of ribosome binding sites in E. coli, Nucleic Acids Res., 22, 1287, 10.1093/nar/22.7.1287 · DOI
  27. Retallack, 2007, Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences, Biotechnol. Lett., 29, 1483, 10.1007/s10529-007-9415-5 · DOI
  28. Golden, 1998, M.R. van Schravendijk, B.J. Sullivan, E.S. Kawasaki, M.S. Osburne, Effect of promoters and signal sequences on the production of secreted HIV-1 gp120 protein in the baculovirus system, Protein Expr. Purif., 14, 8, 10.1006/prep.1998.0926 · DOI
  29. Boyd, 1993, Turbo cloning: a fast, efficient method for cloning PCR products and other blunt-ended DNA fragments into plasmids, Nucleic Acids Res., 21, 817, 10.1093/nar/21.4.817 · DOI
  30. Buchholz, 2001, LoxP-directed cloning: use of Cre recombinase as a universal restriction enzyme, Biotechniques, 31, 906, 10.2144/01314rr02 · DOI
  31. Ng, 2001, Development of a FLP/frt system for generating helper-dependent adenoviral vectors, Mol. Ther., 3, 809, 10.1006/mthe.2001.0323 · DOI
  32. Radulovich, 1998, Modified gateway system for double shRNA expression and Cre/lox based gene expression, BMC Biotechnol., 11, 24, 10.1186/1472-6750-11-24 · DOI
  33. Seibler, 1998, DNA cassette exchange in ES cells mediated by Flp recombinase: an efficient strategy for repeated modification of tagged loci by marker-free constructs, Biochemistry, 37, 6229, 10.1021/bi980288t · DOI
  34. Perehinec, 2007, Construction and evaluation of multisite recombinatorial (Gateway) cloning vectors for Gram-positive bacteria, BMC Mol. Biol., 8, 80, 10.1186/1471-2199-8-80 · DOI
  35. Kwon, 2011, Recombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis, BMC Biochemistry, 12, 17, 10.1186/1471-2091-12-17 · DOI
  36. Szybalski, 1985, Universal restriction endonucleases: designing novel cleavage specificities by combining adapter oligodeoxynucleotide and enzyme moieties, Gene, 40, 169, 10.1016/0378-1119(85)90039-3 · DOI
  37. Szybalski, 1991, Class-IIS restriction enzymes–a review, Gene, 100, 13, 10.1016/0378-1119(91)90345-C · DOI
  38. Baneyx, 1991, Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo, J. Bacteriol., 173, 2696, 10.1128/jb.173.8.2696-2703.1991 · DOI
  39. Park, 1999, Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli strain, Biotechnol. Prog., 15, 164, 10.1021/bp9900108 · DOI
  40. Simmons, 2002, Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies, J. Immunol. Methods, 263, 133, 10.1016/S0022-1759(02)00036-4 · DOI
  41. Thomas, 1997, Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold, Appl. Biochem. Biotechnol., 66, 197, 10.1007/BF02785589 · DOI
  42. Baneyx, 1999, Recombinant protein expression in Escherichia coli, Curr. Opin. Biotechnol., 10, 411, 10.1016/S0958-1669(99)00003-8 · DOI
  43. Narayanan, 2011, Enhancing functional expression of Heterologous Burkholderia lipase in Escherichia coli, Mol. Biotechnol., 47, 130, 10.1007/s12033-010-9320-3 · DOI
  44. Chen, 2003, DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli, Protein. Expr. Purif., 32, 221, 10.1016/S1046-5928(03)00233-X · DOI
  45. Nishihara, 1998, Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli, Appl. Environ. Microbiol., 64, 1694, 10.1128/AEM.64.5.1694-1699.1998 · DOI
  46. Lee, 1992, Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli, J. Biol. Chem., 267, 2849, 10.1016/S0021-9258(19)50659-7 · DOI
  47. Zhang, 2002, Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli, Protein Expr. Purif., 26, 218, 10.1016/S1046-5928(02)00502-8 · DOI
  48. Luan, 2004, High-Throughput Expression of C. elegans Proteins, Genome Res., 14, 2102, 10.1101/gr.2520504 · DOI
  49. Chambers, 2004, High-throughput screening for soluble recombinant expressed kinases in Escherichia coli and insect cells, Protein Expr. Purif., 36, 40, 10.1016/j.pep.2004.03.003 · DOI
  50. Ergin, 2007, Homologous high-throughput expression and purification of highly conserved E. coli proteins, Microb. Cell Fact., 6, 18, 10.1186/1475-2859-6-18 · DOI
  51. Benita, 2006, Analysis of high throughput protein expression in Escherichia coli, Mol. Cell. Proteomics, 5, 1567, 10.1074/mcp.M600140-MCP200 · DOI
  52. Braun, 2002, Proteome-scale purification of human proteins from bacteria, Proc. Natl. Acad. Sci. USA, 99, 2654, 10.1073/pnas.042684199 · DOI
  53. Tang-Feldman, 2002, One-step cloning and expression of Clostridium difficile toxin B gene (tcdB), Mol. Cell Probes, 16, 179, 10.1006/mcpr.2002.0409 · DOI
  54. Voth, 2005, Clostridium difficile toxins: mechanism of action and role in disease, Clin. Microbiol. Rev., 18, 247, 10.1128/CMR.18.2.247-263.2005 · DOI
  55. Lyerly, 1988, Clostridium difficile: its disease and toxins, Clin. Microbiol. Rev., 1, 1, 10.1128/CMR.1.1.1 · DOI
  56. Albesa-Jove, 2010, Four distinct structural domains in Clostridium difficile toxin B visualized using SAXS, J. Mol. Biol., 396, 1260, 10.1016/j.jmb.2010.01.012 · DOI
  57. Kotloff, 2001, Safety and immunogenicity of increasing doses of a Clostridium difficile toxoid vaccine administered to healthy adults, Infect. Immun., 69, 988, 10.1128/IAI.69.2.988-995.2001 · DOI
  58. Roque, 2004, Antibodies and genetically engineered related molecules: production and purification, Biotechnol. Prog., 20, 639, 10.1021/bp030070k · DOI
  59. D.C. Montgomery, Design and Analysis of Experiments, John Wiley and Sons, 2005.
  60. N. Yokoyama, M. Hirata, K. Ohtsuka, Y. Nishiyama, K. Fujii, M. Fujita, K. Kuzushima, T. Kiyono, T. Tsurumi, Co-expression of human chaperone Hsp70 and Hsdj or Hsp40 co-factor increases solubility of overexpressed target proteins in insect cells. Biochimica et Biophysica Acta (BBA) – Gene Struct. Expr. 1493 (2000) 119–124. · DOI
  61. Ahn, 2004, High-level expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone HDJ-1(Hsp40), Protein Expr. Purif., 36, 48, 10.1016/j.pep.2004.03.005 · DOI
  62. Humphreys, 1996, Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab’ fragment expressed in Escherichia coli, FEBS Lett., 380, 194, 10.1016/0014-5793(96)00028-2 · DOI
  63. Zhan, 1999, Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase, Biotechnol. Prog., 15, 1033, 10.1021/bp990083r · DOI
  64. Jin, 2011, Soluble periplasmic production of human granulocyte colony-stimulating factor (G-CSF) in Pseudomonas fluorescens, Protein Expr. Purif., 78, 69, 10.1016/j.pep.2011.03.002 · DOI
  65. Vanz, 2008, Human granulocyte colony stimulating factor (hG-CSF): cloning, overexpression, purification and characterization, Microb. Cell Fact., 7, 13, 10.1186/1475-2859-7-13 · DOI
  66. Phelps, 2007, Inactivation and purification of cowpea mosaic virus-like particles displaying peptide antigens from Bacillus anthracis, J. Virol. Methods, 141, 146, 10.1016/j.jviromet.2006.12.008 · DOI
  67. Zhao, 1995, In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA, Virology, 207, 486, 10.1006/viro.1995.1108 · DOI
  68. Wu, 2010, Soluble expression and purification of the anthrax protective antigen in E coli and identification of a novel dominant-negative mutant N435C, Appl. Microbiol. Biotechnol., 87, 609, 10.1007/s00253-010-2495-5 · DOI
  69. Haslam, 1986, Growth of Clostridium difficile and production of toxins A and B in complex and defined media, J. Med. Microbiol., 21, 293, 10.1099/00222615-21-4-293 · DOI

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Metadata

Authors
Retallack, D. M., Jin, H., & Chew, L.
Venue
Protein Expression and Purification
Publisher
Elsevier BV
Published
2012-02
Volume
81
Issue
2
Pages
157-165
ISSN
1046-5928
DOI
10.1016/j.pep.2011.09.010
Cited by
46
References
0
Language
en
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