medigraphic.com
ISSN 1025-0298 (Digital)
ISSN 1025-028X (Impreso)

2013, Número 2

<< Anterior Siguiente >>

VacciMonitor 2013; 22 (2)


Estrategias de obtención de proteínas recombinantes en Escherichia coli

García J, Santana Z, Zumalacárregui L, Quintana M, González D, Furrazola G, Cruz O

Idioma: Español
Referencias bibliográficas: 50
Paginas: 30-39
Archivo PDF: 108.88 Kb.


RESUMEN

La expresión de proteínas recombinantes se ha favorecido con el uso de Escherichia coli debido a su relativo bajo costo, alta densidad de cultivo, su fácil manipulación genética y a las diversas herramientas biotecnológicas disponibles que son compatibles. En este artículo se presentan algunas estrategias para la expresión de Escherichia coli; se destacan factores genéticos y fisiológicos que incluyen: número de copias del vector de expresión, características del gen, estabilidad del ácido ribonucleico mensajero, promotor empleado, cepa utilizada, composición del medio de cultivo, parámetros de operación en el fermentador y también se abordan la conservación de cepas y la estrategia de cultivo y purificación.


REFERENCIAS (EN ESTE ARTÍCULO)

  1. Ferrer N, Domingo J, Corchero J, Vázquez E, Villaverde A. Microbial factories for recombinant pharmaceuticals. Microbial Cell Factories 2009;8(1):17-8.

  2. Perry Chou C. Engineering cell physiology to enhance recombinant protein production in Escherichia coli. Appl Microbiol Biotechnol 2007;76:521–32.

  3. Jonasson P, Liljeqvist S, Nygren PA, Ståhl S. Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. Biotechnol Appl Biochem 2002;35(2):91- 105.

  4. Choi JH, Keum KC, Lee SY. Production of recombinant proteins by high cell density culture of Escherichia coli. Chemical Engineering Science 2006;61:876-85.

  5. Santana H, Martínez E, Sánchez J C, Moya G, Sosa, R, Hardy E, et al. Molecular characterization of recombinant human interferon alpha-2b produced in Cuba. Biotecnología Aplicada 1999;16(3):154-9.

  6. Lehmann K, Hoffmann S, Neudecker P, Suhr M, Becker W M, Rosch P. High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h2. Protein Expr Purif 2003;31:250-9.

  7. Bessette PH, Aslund F, Beckwith J, Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci USA 1999;96:13703-08.

  8. Schatz G, Dobberstein B. Common principles of protein translocation across membranes. Science 1996;271:1519–26.

  9. Weikert C, Sauer U, Bailer J. An E. coli Host strain useful for efficient overproduction of secreted recombinant protein. Biotech Bioeng 1997;59(3):386-91.

  10. Nordström K, Uhlin B E. Runaway replication plasmids as tools to produce large quantities of proteins from cloned genes in bacteria. Biotechnology 1992;10:661-6.

  11. Bentley WE, Mirjalili N, Andersen DC, Davis RH, Kompala DS. Plasmid-encoded protein: the principal factor in the “metabolic burden” associate with recombinant bacteria. Biotechnol Bioeng 1990;35:668-81.

  12. Lee CP, Li P, Inouye H, Brickman ER, Beckwith J. Genetic studies on the instability of b-galactocidase to be translocated across the Escherichia coli cytoplasmatic membrane. J Bacteriol 1989;171:4609-16.

  13. Kane JF. Effects of rare codon clusters on high-level expressions of heterologous protein in Escherichia coli. Curr. Opin. Biotechnol. 1995;6:494-500.

  14. Bechhofer D. 5¢ m RNA stabilizers. In Belasco JG, Brawerman G, eds. Control of messenger RNA stability. San Diego: Academic Press; 1993. p. 31-52.

  15. Hanning G, Makrides S C. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol 1998; 16:54-60.

  16. Espinosa R, Caballero E, Musacchio A, Silva R. Production of a recombinant, immunogenic protein, P64k, of Neisseria meningitidis in Escherichia coli in fed-batch fermenters. Biotechnology Letters 2002;24(5):343-6.

  17. Chevalet L, Robert A, Gueneau F, Bonnefoy, JY y Ngugen T. Recombinant protein production driven by the tryptophan promoter is tightly controlled in ICONE 200, a new genetically engineered E. coli mutant. Biotechnology and Bioengineering 2000;69(4):351-8.

  18. Götting C, Thierbach G, Pühler A, Kalinowski J. Versatile lowcopy- number plasmids for temperature inducible overexpression of bacterial genes in Escherichia coli. BioTechniques 1998;24:362-6.

  19. Gronenborn B. Overproduction of phage lambda repressor under control of the lac promoter of Escherichia coli. Mol. Gen. Genet. 1976;148:243-50.

  20. Chermojovsky Y, Mory Y, Vaks B, Funstein SI, Segev D, Revel M. Production of human interferon in E. coli under lac and tryplac promoter control. Ann NY Acad. Sci 1983;413:88-96.

  21. Sørensen HP, Mortensen KK. Advanced genetics strategy for recombinant protein expression in Escherichia coli. Journal of Biotechnology 2005;115:113-28.

  22. Jonasson P, Liljeqvist S, Nygren P, Stahl S. Genetic design for facilitated production and recovery of recombinant proteins in E coli Biotechnol. Appl. Biochem 2002;35:91–105.

  23. Organización Mundial de la Salud. Serie de Informes Técnicos. Anexo 1 “Prácticas adecuadas para la fabricación de productos biológicos”. Ginebra: OMS: 1992.

  24. ICH. Quality of Biotechnological Products: Analysis of the expression construct in cells used for production of rDNA derived products (Q5B) 1997. Disponible en: http:// www.ich.org/cache/compo/276-254-1.html.

  25. ISO/TS 11133-1. Part 2 “Practical guidelines on performance testing of culture media”. Sydney, Australia: ISO; 2009.

  26. Tran QH, Unden G. Changes in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation. Eur J Biochem 1998;251(1-2):538-43.

  27. Konstantin B, Naoki N, Toshiomi Y. Glucose feeding strategy accounting for the decreasing oxidative capacity of recombinant E. coli in fed-batch cultivation for phenilalanine production. Journal of Fermentation and Bioenginnering 1990;70(4):253-60.

  28. Monod J. La technique de culture continue, théorie et applications. Ann Inst Past 1950;79:390-410.

  29. Kleman G, Strohl W. Acetate metabolism by Escherichia coli in high-cell-density fermentation. Appl Environ. Microbiol. 1994;60(11) 3952-8.

  30. Lee SY. High cell density culture of Escherichia coli. Tibtech 1996;14:98-105.

  31. Makrides SC. Strategies for achieving high level expression of genes in Escherichia coli. Microbiol Rev 1996;60(3):512-38.

  32. Shimizu N, Fukusono S, Harada Y, Fujimori K, Gotoh K, Yamasaki Y. Mass production of human epidermal growth factor using fed-batch cultures of recombinant Escherichia coli. Biotechnol Bioeng 1991;38(1):37-42.

  33. Markl H, Dubach AC, Ogbonna JC. Cultivation of Escherichia coli to high cell densities in a dialysis reactor. Appl Microbiol Biotechnol 1993;39(1):48-52.

  34. Babu KR. Production of interferon alpha in high cell density cultures of recombinant Escherichia coli and its single step purification from refolded inclusion body proteins. Appl Microbiol Biotechnol 2000;53(6):655-60.

  35. Manderson D, Robert A, Dempster A, Chisti Y. A recombinant vaccine against hydatidosis: production of the antigen in Escherichia coli. J Ind Microbiol Biotechnol 2006;33:173–82.

  36. Luli G W, Strohl WR. Comparison of growth, acetate production and acetate inhibition of Escherichia coli strains in batch and fed batch fermentations. Appl Environ Microbiol 1990;56: 1004-11.

  37. Tripathi NK, Sathyaseelan K, Jana AM, Rao PVL, Kang WK, Park TH. High Yield Production of Heterologous Proteins with Escherichia coli Defence. Science Journal 2009;59(2):137-46.

  38. Lin HY. Determination of the maximum specific uptake capacities for glucose and oxygen in glucose-limited-fed batch cultivation of Escherichia coli. Biotechnol Bioeng 2001;75(5):347-57.

  39. Akesson M, Hagander P, Axelsson J. Avoiding acetate accumulation in Escherichia coli cultures using feedback control of glucose feeding. Biotechnol Bioeng 2001;73(3): 223-30.

  40. Du P, Ye Q, Yu JT. Cultivation integrated with acetate filtration on Escherichia coli. Sheng Wu Gong Cheng Xue Bao; 2000;16(4):528-30.

  41. Zhang WC. High cell density culture of phosphotransacetylase mutants of Escherichia coli BL21(DE3). Sheng Wu Gong Cheng Xue Bao 2001;17(1):59-63.

  42. Beckley K, Verhaert P, van der Wielen LAM, Hubbuch J, Ottens M. Rational and systematic protein purification process development: the next generation. Trends Biotechnol 2009;27(12):673-79.

  43. Gómez R, Madrazo J, González L, Chinea G, Musacchio A, Rodríguez A, et al. Caracterización estructural y funcional de la proteína recombinante P64k de Neisseria meningitidis. Biotecnología Aplicada 1999;16(2):83-7.

  44. Ward W, Swiatek G. Protein Purification. Current Analytical Chemistry 2009;5(2):1-21.

  45. Purifying Challenging Proteins. Principles and Methods. Uppsala, Sweden: GE Healthcare Bio-Sciences; 2007.

  46. Middelberg APJ. Preparative protein refolding. Trends in Biotechnology 2002; 20(10):437-43.

  47. Geng X, Wang C. Protein folding liquid chromatography and its recent developments. Journal of Chromatography B. 2007;849(1):69–80.

  48. Lilie H, Schwarz E, Rudolph R. Advances in refolding of proteins produced in E. coli. Current Opinion in Biotechnology 1998; 9(5):497-501.

  49. Curling J. Process Chromatography: Five Decades of Innovation. BioPharm Int 2007;20 (Suppl. 1):10-20.

  50. Chen R, Huang C, Newton B, Ritter G, Old L, Batt C. Factors affecting endotoxin removal from recombinant therapeutic proteins by anion exchange chromatography. Prot Exp Purif 2009;64:76–81.




2020     |     www.medigraphic.com