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2018, Number 1

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Rev Educ Bioquimica 2018; 37 (1)

Aspectos metodológicos de la expresión de proteínas recombinantes en Escherichia coli

González A, Fillat MF

Language: Spanish
References: 61
Page: 14-27
PDF size: 345.54 Kb.


ABSTRACT

Large amounts of pure, soluble and biologically active proteins are increasingly required in research projects, diagnosis, therapies and industry. Purification of proteins from natural sources usually fails in guarantee the appropriate amount and quality of these biomolecules, and sometimes diminishes the economic feasibility of the process. The advent of recombinant DNA technology in the mid-1970s marked the beginning of modern biotechnology. Current knowledges in genomic, proteomic and bioinformatics have led to an exponentially increase in recombinant protein production. Due to its fast growth and high cell yields in inexpensive media, its wellcharacterized genetics and physiology, as well as its high capability for production of heterologous proteins, the enterobacterium Escherichia coli remains as the system of choice for the production of recombinant proteins in both on a lab scale and in industry. Here, we review the most relevant methodological aspects to be considered in order to ensure successful expression of biologically active recombinant proteins using E. coli as host.


REFERENCES

  1. Jia B, Jeon CO (2016) High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives. Open Biol 6: 160196.

  2. Klammt C, Schwarz D, Lohr F, Schneider B, Dotsch V, Bernhard F (2006) Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J 273: 4141-4153.

  3. Schmidt FR (2004) Recombinant expression systems in the pharmaceutical industry. Appl Microbiol Biotechnol 65: 363-372.

  4. Terpe K (2006) Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 72: 211-222.

  5. Martinez JL, Liu L, Petranovic D, Nielsen J (2012) Pharmaceutical protein production by yeast: towards production of human blood proteins by microbial fermentation. Curr Opin Biotechnol 23: 965-971.

  6. Streatfield SJ (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol J 5: 2-15.

  7. Tiwari S, Verma PC, Singh PK, Tuli R (2009) Plants as bioreactors for the production of vaccine antigens. Biotechnol Adv 27: 449-467.

  8. Jarvis DL (2009) Baculovirus-insect cell expression systems. Methods Enzymol 463: 191-222.

  9. Cregg JM, Tolstorukov I, Kusari A, Sunga J, Madden K, Chappell T (2009) Expression in the yeast Pichia pastoris. Methods Enzymol 463: 169-189.

  10. Lalonde ME, Durocher Y (2017) Therapeutic glycoprotein production in mammalian cells. J Biotechnol 251: 128-140.

  11. Zemella A, Thoring L, Hoffmeister C, Kubick S (2015) Cell-free protein synthesis: pros and cons of prokaryotic and eukaryotic systems. Chembiochem 16: 2420-2431.

  12. Gomez S, Lopez-Estepa M, Fernandez FJ, Suarez T, Vega MC (2016) Alternative eukaryotic expression systems for the production of proteins and protein complexes. Adv Exp Med Biol 896: 167-184.

  13. Rosano GL, Ceccarelli EA (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol 5: 172.

  14. Sorensen HP, Mortensen KK (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115: 113-128.

  15. Peti W, Page R (2007) Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expr Purif 51: 1-10.

  16. Zerbs S, Frank AM, Collart FR (2009) Bacterial systems for production of heterologous proteins. Methods Enzymol 463: 149-168.

  17. Chen R (2012) Bacterial expression systems for recombinant protein production: E. coli and beyond. Biotechnol Adv 30: 1102-1107.

  18. Fedulova N, Hanrieder J, Bergquist J, Emren LO (2007) Expression and purification of catalytically active human PHD3 in Escherichia coli. Protein Expr Purif 54: 1-10.

  19. Jeiranikhameneh M, Moshiri F, Keyhan Falasafi S, Zomorodipour A (2017) Designing signal peptides for efficient periplasmic expression of human growth hormone in Escherichia coli. J Microbiol Biotechnol 27: 1999-2009.

  20. Sahdev S, Khattar SK, Saini KS (2008) Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies. Mol Cell Biochem 307: 249-264.

  21. Hunt I (2005) From gene to protein: a review of new and enabling technologies for multiparallel protein expression. Protein Expr Purif 40: 1-22.

  22. Demain AL, Vaishnav P (2009) Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 27: 297-306.

  23. Singh SM, Panda AK (2005) Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng 99: 303-310.

  24. Sorensen HP, Mortensen KK (2005) Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 4: 1.

  25. Burgess RR (2009) Refolding solubilized inclusion body proteins. Methods Enzymol 463: 259-282.

  26. Krishnan B, Hedstrom L, Hebert DN, Gierasch LM, Gershenson A (2017) Expression and purification of active recombinant human alpha-1 antitrypsin (AAT) from Escherichia coli. Methods Mol Biol 1639: 195-209.

  27. Ma Y, Yu J, Lin J, Wu S, Li S, Wang J (2016) High efficient expression, purification, and functional characterization of native human epidermal growth factor in Escherichia coli. Biomed Res Int 2016: 3758941.

  28. Wang M, Jiang S, Wang Y (2016) Recent advances in the production of recombinant s u b u n i t va c c i n e s i n P i c h i a p a s t o r i s . Bioengineered 7: 155-165.

  29. Kost TA, Condreay JP, Jarvis DL (2005) Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat Biotechnol 23: 567-575.

  30. Kost TA, Kemp CW (2016) Fundamentals of baculovirus expression and applications. Adv Exp Med Biol 896: 187-197.

  31. Niimi T (2012) Recombinant protein production in the eukaryotic protozoan parasite Leishmania tarentolae: a review. Methods Mol Biol 824: 307-315.

  32. Niimi T (2016) Leishmania tarentolae for the production of multi-subunit complexes. Adv Exp Med Biol 896: 155-165.

  33. Ahmad A, Pereira EO, Conley AJ, Richman AS, Menassa R (2010) Green biofactories: recombinant protein production in plants. Recent Pat Biotechnol 4: 242-259.

  34. Thoring L, Dondapati SK, Stech M, Wustenhagen DA, Kubick S (2017) High-yield production of “difficult-to-express” proteins in a continuous exchange cell-free system based on CHO cell lysates. Sci Rep 7: 11710.

  35. Saida F, Uzan M, Odaert B, Bontems F (2006) Expression of highly toxic genes in E. coli: special strategies and genetic tools. Curr Protein Pept Sci 7: 47-56.

  36. Browning DF, Busby SJ (2016) Local and global regulation of transcription initiation in bacteria. Nat Rev Microbiol 14: 638-650.

  37. Tegel H, Ottosson J, Hober S (2011) Enhancing the protein production levels in Escherichia coli with a strong promoter. FEBS J 278: 729-739.

  38. Makrides SC (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 60: 512-538.

  39. Estrem ST, Ross W, Gaal T, Chen ZW, Niu W, Ebright RH, Gourse RL (1999) Bacterial promoter architecture: subsite structure of UP elements and interactions with the carboxyterminal domain of the RNA polymerase alpha subunit. Genes Dev 13: 2134-2147.

  40. Kane JF (1995) Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr Opin Biotechnol 6: 494-500.

  41. Brunelle JL, Green R (2014) One-dimensional SDS-polyacrylamide gel electrophoresis (1D SDS-PAGE). Methods Enzymol 541: 151-159.

  42. Balbas P (2001) Understanding the art of producing protein and nonprotein molecules in Escherichia coli. Mol Biotechnol 19: 251-267.

  43. Galloway CA, Sowden MP, Smith HC (2003) Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase. Biotechniques 34: 524-526, 528, 530.

  44. Costa S, Almeida A, Castro A, Domingues L (2014) Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system. Front Microbiol 5: 63.

  45. Garcia-Fruitos E, Gonzalez-Montalban N, Morell M, Vera A, Ferraz RM, Aris A, Ventura S, Villaverde A (2005) Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb Cell Fact 4: 27.

  46. Nahalka J (2008) Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose- 1-phosphate. J Ind Microbiol Biotechnol 35: 219-223.

  47. Villaverde A, Corchero JL, Seras-Franzoso J, Garcia-Fruitos E (2015) Functional protein aggregates: just the tip of the iceberg. Nanomedicine (Lond) 10: 2881-2891.

  48. Malik A (2016) Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli. 3 Biotech 6: 44.

  49. Choi JH, Lee SY (2004) Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 64: 625-635.

  50. Zhou Y, Lu Z, Wang X, Selvaraj JN, Zhang G (2018) Genetic engineering modification and fermentation optimization for extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 102: 1545-1556.

  51. Albiniak AM, Matos CF, Branston SD, Freedman RB, Keshavarz-Moore E, Robinson C (2013) High-level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin-arginine translocation system in Escherichia coli. FEBS J 280: 3810-3821.

  52. Ryan DP, Tremethick DJ (2016) A dual affinity-tag strategy for the expression and purification of human linker histone H1.4 in Escherichia coli. Protein Expr Purif 120: 160-168.

  53. Malhotra A (2009) Tagging for protein expression. Methods Enzymol 463: 239-258.

  54. Butt TR, Edavettal SC, Hall JP, Mattern MR (2005) SUMO fusion technology for difficultto- express proteins. Protein Expr Purif 43: 1-9.

  55. Zhao X, Li G, Liang S (2013) Several affinity tags commonly used in chromatographic purification. J Anal Methods Chem 2013: 581093.

  56. Rozkov A, Enfors SO (2004) Analysis and control of proteolysis of recombinant proteins in Escherichia coli. Adv Biochem Eng Biotechnol 89: 163-195.

  57. Busso D, Peleg Y, Heidebrecht T, Romier C, Jacobovitch Y, Dantes A, Salim L, Troesch E, Schuetz A, Heinemann U, Folkers GE, Geerlof A, Wilmanns M, Polewacz A, Quedenau C, Bussow K, Adamson R, Blagova E, Walton J, Cartwright JL, Bird LE, Owens RJ, Berrow NS, Wilson KS, Sussman JL, Perrakis A, Celie PH (2011) Expression of protein complexes using multiple Escherichia coli protein coexpression systems: a benchmarking study. J Struct Biol 175: 159-170.

  58. Diebold ML, Fribourg S, Koch M, Metzger T, Romier C (2011) Deciphering correct strategies for multiprotein complex assembly by co-expression: application to complexes as large as the histone octamer. J Struct Biol 175: 178-188.

  59. Haffke M, Marek M, Pelosse M, Diebold ML, Schlattner U, Berger I, Romier C (2015) Characterization and production of protein complexes by co-expression in Escherichia coli. Methods Mol Biol 1261: 63-89.

  60. Schwarz D, Dotsch V, Bernhard F (2008) Production of membrane proteins using cell-free expression systems. Proteomics 8: 3933-3946.

  61. Kamionka M (2011) Engineering of therapeutic proteins production in Escherichia coli. Curr Pharm Biotechnol 12: 268-274.




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