Bacterial overexpression of the human interleukin-2 in insoluble form via the pET Trx fusion system

Document Type: Short Paper

Authors

1 Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-154, Tehran, I.R. Iran.

2 National Cell Bank of Iran, Pasteur Institute, P.O. Box 1316943551, Tehran, I.R. Iran.

3 Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115- 154,Tehran, I.R. Iran.

4 Biotechnology Group of Chemical Engineering, Faculty of Engineering, Tarbiat Modares University, P.O. Box 14115-143, Tehran, I.R. Iran.

5 Department of Biology, Alzahra University, P.O. Box 1993891176, Tehran, I.R. Iran.

6 Department of Medical Genetics, National Institute of Genetic Engineering and Biotechnology, P.O. Box 14155-6343, Tehran, I.R. Iran.

7 Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-154, Tehran, I.R. Iran.

Abstract

Selection of a system for successful recombinant protein production is important. The aim of this study was
to produce high levels of human interleukin-2 (hIL-2) in soluble form. To this end, the pET32a vector in
Escherichia coli BL21 (DE3) was used as an expression system, since it was previously used for the production
of mouse IL-2 in soluble form. The results indicated that contrary to expectations, the expressed protein
was in the form of inclusion bodies and perhaps amino acid differences between human and mouse IL-
2 should be determinant. The hIL-2 protein is a small peptide, therefore its recovery as a biologically functional protein by the process of refolding may be feasible and could lead to high yields at the industrial scale.

Keywords