Improved periplasmic production of biologically active murine interleukin-2 in Escherichia coli through a single amino acid change at the cleavage site

Process Biochemistry

Volumn 41, Issue 6, 2006, Pages 1343-1346

  Robbens, Johan ^a,b   De Coen, Wim ^b   Fiers, Walter ^a   Remaut, Erik ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b UNIVERSITY OF ANTWERP   (Belgium)

Author keywords

E. coli; High level production; Interleukin 2; Periplasm; Recombinant; Signal peptide

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BODY FLUIDS; CELL CULTURE; PROTEINS;

HIGH-LEVEL PRODUCTION; INTERLEUKIN-2; PERIPLASM; SIGNAL PEPTIDE;

ESCHERICHIA COLI;

ESCHERICHIA COLI; MURINAE;

EID: 33646107403     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2006.01.009     Document Type: Article

References (26)

1. Dinarello C.A., Sheldon T., and Wolff M. As we commemorate the 10th anniversary of the clonings of IL-1 alpha and IL-1 beta. Eur Cytokine Netw 5 (1994) 513-516
2. Dermott D.F., and Atkins M.B. Application of IL-2 and other cytokines in renal cancer. Expert Opin Biol Ther 4 (2004) 455-468
3. Bleumer I., Oosterwijk E., De Mulder P., and Mulders P.F. Immunotherapy for renal cell carcinoma. Eur Urol 44 (2003) 65-75
4. Clegg A., Williamson P., Biti R., Cooper D., Emery S., Carr A., et al. Chemokine receptor genotype and response to interleukin-2 therapy in HIV-1-infected individuals. Clin Immunol 106 (2003) 36-40
5. Gaffen S.L., and Liu D. Overview of interleukin-2 function, production and clinical applications. Cytokine 28 (2004) 109-123
6. Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 11 (2004) 1399-1408
7. Mertens N., Remaut E., and Fiers W. Versatile, multi-featured plasmids for high-level expression of heterologous genes in Escherichia coli: overproduction of human and murine cytokines. Gene 164 (1995) 9-15
8. Badyakina A.O., and Nesmeyanova M.A. Biogenesis and secretion of overproduced protein in recombinant strains of Escherichia coli. Process Biochem 40 (2005) 509-518
9. Mergulhao F.J., Summers D.K., and Monteiro G.A. Recombinant protein secretion in Escherichia coli. Biotechnol Adv 23 (2005) 177-202
10. Holland I.B., Mackman N., and Nicaud J.M. Secretion of proteins from bacteria. Bio/Technology 4 (1986) 427-431
11. Halfmann G., Brailly H., Bernadac A., Montero-Julian F.A., Lazdunski C., and Baty D. Targeting of interleukin-2 to the periplasm of Escherichia coli. J Gen Microbiol 139 (1993) 2465-2473
12. Smith K.A. Interleukin 2. Annu Rev Immunol 2 (1984) 319-333
13. Guisez Y., Demolder J., Mertens N., Raeymaekers A., Plaetinck G., Robbens J., et al. High-level expression, purification, and renaturation of recombinant murine interleukin-2 from Escherichia coli. Protein Expr Purif 4 (1993) 240-246
14. Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227 (1970) 680-685
15. Gillis S., Ferm M.M., Ou W., and Smith K.A. T cell growth factor: parameters of production and a quantitative microassay for activity. J Immunol 120 (1978) 2027-2032
16. Rossio J.L., Thurman G.B., Long C., Vargosko A., and Pinsky C. The BRMPIL-2 reference reagent. Lymphokine Res 5 S (1986) 8-13
17. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning-A Laboratory Manual. 2nd ed. (1989), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
18. Bauw G., Van den Bulcke M., Van Damme J., Puype M., Van Montagu M., and Vandekerckhove J. Protein-electroblotting on polybase-coated glass-fiber and polyvinylidene difluoride membranes: an evaluation. J Protein Chem 7 (1988) 194-196
19. Robbens J., Raeymaekers A., Steidler L., Fiers W., and Remaut E. Production of soluble and active recombinant Murine interleukin-2 in Escherichia coli: high level expression, kil-induced release, and purification. Protein Expr Purif 4 (1995) 481-486
20. van Kimmenade A., Dang W., and Kastelein R.A. Secretion of murine and human interleukin-2 by Escherichia coli. J Biotechnol 11 (1989) 11-24
21. Schein C.H. Production of soluble recombinant proteins in bacteria. Bio/Technology 7 (1989) 1141-1149
22. Bakholdina S.I., Sanina N.M., Krasikova I.N., Popova O.B., and Solov'eva T.F. The impact of abiotic factors (temperature and glucose) on physicochemical properties of lipids from Yersinia pseudotuberculosis. Biochimie 86 (2004) 875-881
23. Ullers R.S., Luirink J., Harms N., Schwager F., Georgopoulos C., and Genevaux P. SecB is a bona fide generalized chaperone in Escherichia coli. Proc Natl Acad Sci USA 101 (2004) 7583-7588
24. Guisbert E., Herman C., Lu C.Z., and Gross C.A. A chaperone network controls the heat shock response in E. coli. Genes Dev 15 (2004) 2812-2821
25. Kumamoto C.A., and Beckwith J. Evidence for specificity at an early step in protein export in Escherichia coli. J Bacteriol 163 (1985) 267-274
26. Collet J.F., and Bardwell J.C. Oxidative protein folding in bacteria. Mol Microbiol 44 (2002) 1-8