Journal of Pure and Applied MicrobiologyVol. 7 No. 4

Codon Optimization, Cloning and Expression of Interleukin 11 in Two Different E. coli Systems

Nima Montazeri-Najafabady1,2, Younes Ghasemi1,2,*, Mohammad Ali Mobasher1,2, Abdollah Ghasemian1,2, Sara Rasoul-Amini1,2,3 and Sirus Ebrahimi4

1Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Shiraz University of Medical Sciences, P.O. Box 71345-1583, Shiraz, Iran. 2Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, P.O. Box 71345-1583, Shiraz, Iran. 3Department of Medicinal Chemistry, Faculty of Pharmacy, Shiraz University of Medical Sciences, P.O. Box 71345-1583, Shiraz, Iran. 4Chemical Engineering Faculty, Sahand University of Technology, P.O Box 51335-1996, Tabriz, Iran.

Received on 08 January 2013 and accepted on 25 Feburary 2013

 

ABSTRACT

Interleukin (IL)-11 is a multifunctional cytokine that stimulates hematopoietic progenitor cells and exerts a series of important immunomodulatory effects. Recombinant human interleukin-11 (rhIL-11) has been shown to increase platelet counts in animals and humans and is the only drug approved for use in chemotherapy-induced thrombocytopenia (CIT). rhIL-11 is 19 kDa protein (1) that lacks the N-terminal proline in compare with wild type and has been produced in recombinant E. coli. A synthetic gene of human interleukin 11 was designed, codon optimized, cloned and expressed in E.coli BL21 (DE3) and E. coli Rosetta (DE3) using a pET-15b expression vector. In this study we compared two strategies for better expression of heterologus protein by using two different E. coli systems. As the results show, expression of codon optimized 6His-interleukin 11 in E. coli Rosetta (DE3) was better in comparison with E. coli BL21 (DE3). Not only codon optimization, but appropriate strain selection has a great effect on recombinant protein production in E. coli.

Keywords : Recombinant Human Interleukin 11, Escherichia coli, Codon Bias, Chemotherapy-Induced Thrombocytopenia, Strain Selection.