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Title: Enhanced soluble expression and effective purification of recombinant human interleukin-11 by SUMO fusion in Escherichia coli
Authors: Nguyen, Thi-Quy
Duong, Thu-Huong
Dang, Thi-Ngoc-Ha
Le, Ngoc-Giang
Le, Quynh-Giang
Do, Thi-Huyen
Nguyen, Van-Do
Le, Thi-Thu-Hong
Truong, Nam-Hai
Keywords: Human interleukin-11;SUMO fusion;Escherichia coli;Recombinant protein;Selective precipitation
Issue Date: Oct-2018
Publisher: NISCAIR-CSIR, India
Abstract: Human interleukin-11 is a multifunctional cytokine applied for the clinical treatment of thrombocytopenia. However, IL-11 has been considered a difficult protein in to express in an Escherichia coli expression system. Here, we demonstrate a suitable construction for high production of recombinant human interleukin-11 (rhIL-11) in E. coli. An optimized codon gene encoding human IL-11 was inserted in-frame with the small ubiquitin like modifier (SUMO) protein in the pE-SUMO3 vector. The SUMO IL-11 fusion protein was entirely expressed in soluble form and reached 31.6% of total soluble protein in E. coli. The rhIL-11 protein with a purity of over 99% was obtained at high protein yields of 320 mg rhIL-11 per liter of bacterial culture. Bioactivity of rhIL-11, as determined by proliferation of a TF-1 cytokine-dependent cell line, was 4.17 x 105 unit/mg, similar to the activity of the natural protein. Interestingly, the rhIL-11 was purified easily and effectively due to its selective precipitation from the reaction mixture. To the best of our knowledge, this is the first report demonstrating self-aggregating recombinant protein after cleavage from SUMO. Thus, expression of rhIL-11 fused with SUMO yielded greatly increased soluble production and convenient purification, and could offer a potential drug candidate for deployment in clinical trials.
Page(s): 579-585
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections:IJBT Vol.17(4) [October 2018]

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