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  • Công bố khoa học và công nghệ Việt Nam

62.37

Công nghệ sinh học công nghiệp

Nguyễn Thị Quý, Lê Ngọc Giang, Lê Quỳnh Giang, Dương Thu Hương, Đặng Thị Ngọc Hà, Đỗ Thị Huyền(1), Lê Thị Thu Hồng, Trương Nam Hải

Biểu hiện Interleukin-11 người tái tổ hợp dạng tan trong tế bào Escherichia Coli

Expression of recombinant human Interleukin-ll as soluble form in Escherichia coli

Công nghệ Sinh học

2014

3

417-422

1811-4989

Human Interleukin-11 (hIL-11) is a multifunctional cytokine which modulates the proliferation, differentiation and maturation of hematopoietic cells. Recombinant hIL-11 is the first interleukin approved by Food and Drug Administration (FDA) to administer to patients with low platelet counts. In the previous paper, the authors reported the result of hlL-11 expression into the periplasm of Escherichia coli (E. coli) BL21 with PelB leader. However, the recombinant protein produced at very low level. Here, the authors show the result of hIL-11 expression in a fusion form with SUMO protein (Small Ubiquitin-like Modifier) in E. coli Rosetta 2. SUMO modulates protein structure and function by covanlently binding to the lysine side chains of the target proteins. A gene fragment coding for hIL-11 protein was optimized for codon adaption in E. coli. The 9ptimized gene was inserted into a SUMOpr03 vector and transformed into E. coli Rosetta 2 to express recombinant protein in fusion form with SUMO. The result showed that a strong band of 36 kDa derived from the' fusion protein SUMO-IL 11 was well expressed in the host cells. Importantly, the fusion protein was mainly present in the supernatant phase of the cell lysis.

TTKHCNQG, CVv 262