2013, Number 2
<< Back Next >>
VacciMonitor 2013; 22 (2)
Strategies to obtain recombinant proteins in Escherichia coli
García J, Santana Z, Zumalacárregui L, Quintana M, González D, Furrazola G, Cruz O
Language: Spanish
References: 50
Page: 30-39
PDF size: 108.88 Kb.
ABSTRACT
Recombinant protein expression has been favored by the use of
Escherichia coli due to its relatively low costs,
high-density culture, easy genetic manipulation and also to compatible biotechnological tools. Strategies for
recombinant expression in
E. coli are presented in this paper. Genetic and physiologic factors are presented:
number of copies of the expression vector, characteristic of the gene, ribonucleic acid (messenger) stability,
promoter, host strain, clone stability, composition of the cultivation media, operation parameters in the bioreactor
and cultivation and purification strategies.
REFERENCES
Ferrer N, Domingo J, Corchero J, Vázquez E, Villaverde A. Microbial factories for recombinant pharmaceuticals. Microbial Cell Factories 2009;8(1):17-8.
Perry Chou C. Engineering cell physiology to enhance recombinant protein production in Escherichia coli. Appl Microbiol Biotechnol 2007;76:521–32.
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.
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.
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.
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.
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.
Schatz G, Dobberstein B. Common principles of protein translocation across membranes. Science 1996;271:1519–26.
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.
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.
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.
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.
Kane JF. Effects of rare codon clusters on high-level expressions of heterologous protein in Escherichia coli. Curr. Opin. Biotechnol. 1995;6:494-500.
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.
Hanning G, Makrides S C. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol 1998; 16:54-60.
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.
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.
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.
Gronenborn B. Overproduction of phage lambda repressor under control of the lac promoter of Escherichia coli. Mol. Gen. Genet. 1976;148:243-50.
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.
Sørensen HP, Mortensen KK. Advanced genetics strategy for recombinant protein expression in Escherichia coli. Journal of Biotechnology 2005;115:113-28.
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.
Organización Mundial de la Salud. Serie de Informes Técnicos. Anexo 1 “Prácticas adecuadas para la fabricación de productos biológicos”. Ginebra: OMS: 1992.
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.
ISO/TS 11133-1. Part 2 “Practical guidelines on performance testing of culture media”. Sydney, Australia: ISO; 2009.
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.
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.
Monod J. La technique de culture continue, théorie et applications. Ann Inst Past 1950;79:390-410.
Kleman G, Strohl W. Acetate metabolism by Escherichia coli in high-cell-density fermentation. Appl Environ. Microbiol. 1994;60(11) 3952-8.
Lee SY. High cell density culture of Escherichia coli. Tibtech 1996;14:98-105.
Makrides SC. Strategies for achieving high level expression of genes in Escherichia coli. Microbiol Rev 1996;60(3):512-38.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Ward W, Swiatek G. Protein Purification. Current Analytical Chemistry 2009;5(2):1-21.
Purifying Challenging Proteins. Principles and Methods. Uppsala, Sweden: GE Healthcare Bio-Sciences; 2007.
Middelberg APJ. Preparative protein refolding. Trends in Biotechnology 2002; 20(10):437-43.
Geng X, Wang C. Protein folding liquid chromatography and its recent developments. Journal of Chromatography B. 2007;849(1):69–80.
Lilie H, Schwarz E, Rudolph R. Advances in refolding of proteins produced in E. coli. Current Opinion in Biotechnology 1998; 9(5):497-501.
Curling J. Process Chromatography: Five Decades of Innovation. BioPharm Int 2007;20 (Suppl. 1):10-20.
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.