Expression of the Soluble Extracellular Domain of Human Thrombopoietin Receptor Using a Maltose-Binding Protein-Affinity Fusion System

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  • Zhang Qing
    Biotechnology Research Center, Key Laboratory of Gene Engineering of the Education Ministry, Zhongshan University
  • Pan Rui-Min
    Biotechnology Research Center, Key Laboratory of Gene Engineering of the Education Ministry, Zhongshan University
  • Ge Yi-Chen
    Biotechnology Research Center, Key Laboratory of Gene Engineering of the Education Ministry, Zhongshan University
  • Xu Peilin
    Biotechnology Research Center, Key Laboratory of Gene Engineering of the Education Ministry, Zhongshan University

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The thrombopoietin (TPO) receptor (Mpl) belongs to the family of ligand-dependent cytokine receptors and plays a functional role in regulating platelet production. The signaling capacity largely depends on the binding of TPO to the extracellular domains of the TPO receptor (Mpl-EC). Because the expression level of Mpl in human tissue is very low, studies on the functional and spatial characteristics of its ligand-binding sites have been limited. In the present study, we report the expression and purification of Mpl-EC as a fusion with the maltose-binding protein (MBP), designated MBP-Mpl-EC. MBP-Mpl-EC was expressed in the cytoplasm of Escherichia coli as a soluble fusion protein. Specific binding of TPO to purified MBP-Mpl-EC was demonstrated by a dot-blot assay and surface plasmon resonance. We conclude that bacterial expression of MBP-Mpl-EC yields large amounts of protein with correct folding and that it can be used for further structure and function analyses.

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