Optimization of protein expression systems for modern drug discovery

References

• McPherson A. Protein crystallization in the structural genomics era. J. Struct. Funct. Genomics5(1–2), 3–12 (2004).
   PubMedGoogle Scholar
• Mayr LM. Tackling the chemo-genomic space by novel screening technologies: monograph of ESRF Workshop 58. In: Chemical Genomics: Small Molecule Probes to Study Cellular Function. Jaroch S, Weinmann H (Eds.), Springer Verlag, Weinheim, Germany, 111–173 (2006).
   Google Scholar
• Christendat D, Yee A, Dharamsi A et al. Structural proteomics of an archaeon. Nature Struct. Biol.7, 903–909 (2000).
   PubMedGoogle Scholar
• Roodveldt C, Aharoni A, Tawfik DS. Directed evolution of proteins for heterologous expression and stability. Curr. Opin. Struct. Biol.15, 50–56 (2005).
   PubMedGoogle Scholar
• Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol.60, 523–533 (2003).
   PubMed Web of Science ®Google Scholar
• Butt TR, Edavettal SC, Hall JP, Mattern MR. SUMO fusion technology for difficult-to-express proteins. Protein Expr. Purif.43, 1–9 (2005).
   PubMed Web of Science ®Google Scholar
• Sorensen HP, Sperling-Petersen HU, Mortensen KK. A favorable solubility partner for the recombinant expression of streptavidin. Protein Expr. Purif.32, 252–259 (2003).
   PubMedGoogle Scholar
• Kohli BM, Ostermeier C. A rubredoxin based system for screening of protein expression conditions and on-line monitoring of the purification process. Protein Expr. Purif.28, 362–367 (2003).
   PubMedGoogle Scholar
• Liu Y, Zhao TJ, Yan YB, Zhou HM. Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr. Purif.44, 155–161 (2005).
   PubMed Web of Science ®Google Scholar
• Chatterjee DK, Esposito D. Enhanced soluble protein expression using two new fusion tags. Protein Expr. Purif.46, 122–129 (2006).
   PubMedGoogle Scholar
• Hammarström M, Hellgren N, Van der Berg S et al. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli.Prot. Sci.11, 313–321 (2002).
   PubMed Web of Science ®Google Scholar
• Shih YP, Kung WM, Chen JC et al. High-throughput screening of soluble recombinant proteins Prot. Sci.11, 1714–1719 (2002).
   PubMedGoogle Scholar
• Davis GD, Elisee C, Newham DM, Harrison RG. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotech. Bioeng.65, 382–388 (1999).
   PubMed Web of Science ®Google Scholar
• Dyson MR, Shadbolt PS, Vincent KJ et al. Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotechnology4, 32 (2004).
   PubMed Web of Science ®Google Scholar
• Nallamsetty S, Waugh DS. Solubility-enhancing protein MBP and NusA play a passive role in the folding of their fusion partner. Protein Expr. Purif.45, 175–182 (2006).
   PubMed Web of Science ®Google Scholar
• Bach H, Mazor Y, Shaky S et al. Escherichia coli maltose binding protein as a molecular chaperone for recombinant intracellular single-chain antibodies. J. Mol. Biol.312, 79–93 (2001).
   PubMed Web of Science ®Google Scholar
• Arnau J, Lauritzen C, Petersen GE, Pedersen J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr. Purif.48, 1–13 (2006).
   PubMed Web of Science ®Google Scholar
• Qing G, Ma L-C, Khorchid A et al. Cold-shock induced high-yield expression protein production in Escherichia coli. Nat. Biotechnol.22, 877–882 (2004).
   PubMed Web of Science ®Google Scholar
• Nishihiara K, Kanemori M, Kitagawa M et al. Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisted refolding of an allergen from Japanese cedar pollen, Cryi2, in Escherichia coli. Appl. Environ. Microbiol.64, 1694–1699 (1999).
   Google Scholar
• Xu Y, Weng CL, Narayanan N et al. Chaperone-mediated folding and maturation of the penicillin acylase precursor in the cytoplasm of Escherichia coli. Appl. Environ. Microbiol.71, 6247–6253 (2005).
   PubMedGoogle Scholar
• Sung-Gun K, Dae-Hyuk K, Dae-Hee L et al. Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expr. Purif.41, 426–432 (2005).
   PubMedGoogle Scholar
• Ferrer M, Chernikova TN, Yakimov MM et al. Chaperonins govern growth of Escherichia coli at low temperatures. Nat. Biotechnol.21, 1266–1267 (2003).
   PubMed Web of Science ®Google Scholar
• Strocchi M, Ferrer M, Timmis KN, Golyshin PN. Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones. Proteomics6, 193–206 (2006).
   PubMed Web of Science ®Google Scholar
• Braun P, Ju Y, Halleck A et al. Proteome-scale purification of human proteins from bacteria. Proc. Natl Acad. Sci. USA99, 2654–2659 (2002).
   PubMed Web of Science ®Google Scholar
• Knaust RKC, Nordlund P. Screening for soluble expression of recombinant proteins in a 96-well format. Anal. Biochem.297, 79–85 (2001).
   PubMedGoogle Scholar
• Scheich C, Leitner D, Sievert V et al. Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis. BMC Struct. Biol.4, 4 (2004).
   PubMedGoogle Scholar
• Lin CT, Moore PA, Auberry DL et al. Automated purification of recombinant proteins: combining high-throughput with high yield. Protein Expr. Purif.47, 16–24 (2006).
   PubMedGoogle Scholar
• Tobbell DA, Middleton BJ, Raines S et al. Identification of in vitro folding conditions for procathepsin S and cathepsin S using fractional factorial screens. Protein Expr. Purif.24, 242–252 (2002).
   PubMedGoogle Scholar
• Vincentelli R, Canaan S, Campanacci V et al. High-throughput automated refolding screening of inclusion bodies. Prot. Sci.22, 2782–2792 (2004).
   Google Scholar
• Willis MS, Hogan JK, Prabhakar P et al. Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions. Prot. Sci.14, 1818–1826 (2005).
   PubMedGoogle Scholar
• Altamirano MM, Consuelo G, Possani LD, Fersht AR. Oxidative refolding chromatography of the scorpion toxin Cn5. Nat. Biotechnol.17, 187–191 (1999).
   PubMed Web of Science ®Google Scholar
• Gao YG, Guan YX, Yao SJ, Cho MG. On-column refolding of recombinant human interferon-γ with an immobilized chaperone fragment. Biotechn. Prog.19, 915–920 (2003).
   PubMedGoogle Scholar
• SchonerBE, Bramlett KS, Guo H, Burris TP. Reconstitution of functional nuclear receptor proteins using high pressure refolding. Mol. Gen. Metabol.84, 318–322 (2005).
   Google Scholar
• Lee SH, Carpenter JF, Chang BS et al. Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure. Prot. Sci.15, 304–313 (2006).
   PubMed Web of Science ®Google Scholar
• Ikonomou L, Schneider YJ, Agathos SN. Insect cell culture for industrial production of recombinant proteins. Appl. Microbiol. Biotechnol.62, 1–20 (2003).
   PubMed Web of Science ®Google Scholar
• Philipps B, Forstner M, Mayr LM. Baculovirus expression system for magnetic sorting of infected cells and enhanced titer determination. Biotechniques36, 80–83 (2004).
   PubMedGoogle Scholar
• Philipps B, Rotmann D, Wicki M et al. Time reduction and process optimization of the baculovirus expression system for more efficient recombinant protein production in insect cells. Protein Expr. Purif.42, 211–218 (2005).
   PubMed Web of Science ®Google Scholar
• Chen YJ, Chen WS, Wu TY. Development of a bicistronic baculovirus expression vector by the Rhopalosiphum padi virus 5´ internal ribosome entry site. Biochem. Biophys. Res. Commun.335, 616–623 (2005).
   PubMedGoogle Scholar
• Berger I, Fitzgerald DJ, Richmond TJ. Baculovirus expression system for heterologous multiprotein complexes. Nat. Biotechnol.22, 1583–1587 (2004).
   PubMedGoogle Scholar
• Jarvis DL. Developing baculovirus–insect cell expression systems for humanized recombinant glycoprotein production. Virology310, 1–7 (2003).
   PubMed Web of Science ®Google Scholar
• Philipps B, Forstner M, Mayr LM. A baculovirus expression vector system for simultaneous protein expression in insect and mammalian cells. Biotechnol. Prog.21, 708–711 (2005).
   PubMed Web of Science ®Google Scholar
• Kost TA, Condreay JP, Jarvis DL. Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol.23, 567–575 (2005).
   PubMed Web of Science ®Google Scholar
• McCall EJ, Danielsson A, Hardern IM et al. Improvements to the throughput of recombinant protein expression in the baculovirus/insect cell system. Protein Expr. Purif.42, 29–36 (2005).
   PubMedGoogle Scholar
• Hunt I. From gene to protein: a review of new and enabling technologies for multi-parallel protein expression. Protein Expr. Purif.40, 1–22 (2005).
   PubMed Web of Science ®Google Scholar
• Bahia D, Cheung R, Buchs M et al. Optimisation of insect cell growth in deep-well blocks: development of a high-throughput insect cell expression screen. Protein Expr. Purif.39, 61–70 (2005).
   PubMedGoogle Scholar
• MassieB, Dionne J, Lamarche N et al. Improved adenovirus vector provides herpes simplex virus ribonucleotide reductase R1 and R2 subunits very efficiently. Biotechnology (NY)13, 602–608 (1995).
   PubMedGoogle Scholar
• Garnier A, Cote J, Nadeau I et al. Scale up of the adenovirus expression system for the production of recombinant protein in human 293S cells. Cytotechnology15, 145–155 (1994).
   PubMed Web of Science ®Google Scholar
• Pialoux G, Excler JL, Riviere Y et al. A prime-boost approach to HIV preventive vaccine using a recombinant canarypox virus expressing glycoprotein 160 (MN) followed by a recombinant glycoprotein 160 (MN/LAI). AIDS Res. Hum. Retroviruses11, 373–381 (1995).
   PubMed Web of Science ®Google Scholar
• Falkner FG, Turecek PL, MacGillivray RT et al. High level expression of active human prothrombin in a vaccinia virus expression system. Thromb. Haemost.68, 119–124 (1992).
   PubMedGoogle Scholar
• Liljestrom P, Garoff H. A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Biotechnology (NY)9, 1356–1361 (1991).
   PubMedGoogle Scholar
• LundstromK. Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim. Biophys. Acta1610, 90–96 (2003).
   PubMed Web of Science ®Google Scholar
• Hassaine G, Wagner R, Kempf J et al. Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells. Protein Expr. Purif.45, 343–351 (2006).
   PubMedGoogle Scholar
• Lundstrom K. Semliki Forest virus vectors for large-scale production of recombinant proteins. Methods Mol. Med.76, 525–543 (2003).
   PubMedGoogle Scholar
• Geisse S, Henke M. Large-scale transient transfection of mammalian cells: a newly emerging attractive option for recombinant protein production. J. Struct. Funct. Genomics6, 165–170 (2005).
   PubMedGoogle Scholar
• Al-Fageeh MB, Marchant RJ, Carden MJ, Smales CM. The cold-shock response in cultured mammalian cells: harnessing the response for the improvement of recombinant protein production. Biotechnol. Bioeng.93, 829–835 (2006).
   PubMedGoogle Scholar
• Beer C, Buhr P, Hahn H et al. Gene expression analysis of murine cells producing amphotropic mouse leukaemia virus at a cultivation temperature of 32 and 37 degrees C. J. Gen. Virol.84, 1677–1686 (2003).
   PubMedGoogle Scholar
• Ivanova L, Brandli J, Saudan P, Bachmann MF. Hybrid Sindbis/Epstein-Barr virus episomal expression vector for inducible production of proteins. Biotechniques39, 209–212 (2005).
   PubMedGoogle Scholar
• Kigawa T, Yabuki T, Yoshida Y et al. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett.442, 15–19 (1999).
   PubMed Web of Science ®Google Scholar
• Yokoyama S. Protein expression systems for structural genomics and proteomics. Curr. Opin. Chem. Biol.7, 39–43 (2003).
   PubMed Web of Science ®Google Scholar
• Yee A, Chang X, Pineda-Lucena A et al. An NMR approach to structural proteomics. Proc. Natl Acad. Sci. USA99, 1825–1830 (2002).
   PubMed Web of Science ®Google Scholar
• Guignard L, Ozawa K, Pursglove SE et al. NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach. FEBS Lett.524, 159–162 (2002).
   PubMedGoogle Scholar
• Elbaz Y, Steiner-Mordoch S, Danieli T, Schuldiner S. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl Acad. Sci. USA101, 1519–1524 (2004).
   PubMedGoogle Scholar
• Hendrickson WA, Horton JR, LeMaster DM. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J.9, 1665–1672 (1990).
   PubMed Web of Science ®Google Scholar
• Kigawa T, Yamaguchi-Nunokawa E, Kodama K et al. Selenomethionine incorporation into a protein by cell-free synthesis. J. Struct. Funct. Genomics2, 29–35 (2002).
   PubMedGoogle Scholar
• Shimizu Y, Inoue A, Tomari Y et al. Cell-free translation reconstituted with purified components. Nat. Biotechnol.19, 751–755 (2001).
   PubMed Web of Science ®Google Scholar
• He M, Taussig MJ. DiscernArray technology: a cell-free method for the generation of protein arrays from PCR DNA. J. Immunol. Methods274, 265–270 (2003).
   PubMed Web of Science ®Google Scholar
• Jiang X, Ookubo Y, Fujii I et al. Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system. FEBS Lett.514, 290–294 (2002).
   PubMed Web of Science ®Google Scholar
• Sawasaki T, Ogasawara T, Morishita R, Endo Y. A cell-free protein synthesis system for high-throughput proteomics. Proc. Natl Acad. Sci. USA99, 14652–14657 (2002).
   PubMed Web of Science ®Google Scholar
• Tymms MJ (Ed.) In vitro transcription and translation protocols. In: Methods in Molecular Biology. Vol. 37. Humana Press, NJ, USA (1995).
   Google Scholar
• EndoY, Sawasaki T. High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system. J. Struct. Funct. Genomics5, 45–57 (2004).
   PubMedGoogle Scholar
• Tarui H, Murata M, Tani I et al. Establishment and characterization of cell-free translation/glycosylation in insect cell (Spodoptera frugiperda 21) extract prepared with high pressure treatment. Appl. Microbiol. Biotechnol.55, 446–453 (2001).
   PubMedGoogle Scholar
• Jackson AM, Boutell J, Cooley N, He M. Cell-free protein synthesis for proteomics. Brief Funct. Genomic. Proteomic.2, 308–319 (2004).
   PubMedGoogle Scholar
• Davis BG. Biochemistry. Mimicking post-translational modifications of proteins. Science303, 480–482 (2004).
   PubMedGoogle Scholar
• Katzen F, Chang G, Kudlicki W. The past, present and future of cell-free protein synthesis. Trends Biotechnol.23, 150–156 (2005).
   PubMed Web of Science ®Google Scholar
• Acton TB, Gunsalus KC, Xiao R et al. Robotic cloning and Protein Production Platform of the Northeast Structural Genomics Consortium. Methods Enzymol.394, 210–243 (2005).
   PubMed Web of Science ®Google Scholar