Production and characterization of human CTLA4Ig expressed in transgenic rice cell suspension cultures.
作者： Song-Jae Lee , Cheon-Ik Park , Mi-Young Park , Hahn-Sun Jung , Wuk-Sang Ryu
DOI: 10.1016/J.PEP.2006.08.019
关键词: Expression vector 、 Genetically modified rice 、 Transgene 、 Fusion protein 、 Recombinant DNA 、 Transformation (genetics) 、 Molecular biology 、 Affinity chromatography 、 Protein A 、 Biology
摘要: Abstract Human cytotoxic T-lymphocyte antigen 4-immunoglobulin (hCTLA4Ig) fusion protein, a novel immunosuppressive agent, was expressed in transgenic rice cell suspension culture and its characteristics vitro activities were investigated. The expression vector pMYN409 constructed to express hCTLA4Ig under the control of α-amylase 3D (RAmy3D) promoter. Transgenic calli prepared by particle bombardment mediated transformation screened for using ELISA. Under induction condition sugar starvation, suspension-cultured cells secreted into media up 31.4 mg/L flask culture. rice-derived (hCTLA4Ig P ) purified from with affinity chromatography protein A compared CHO-derived M ). Recombinant has molecular weight ∼50 kDa on SDS–PAGE reducing condition, which is little different that probably due difference carbohydrate chain structures. Purified biologically active confirmed suppress T-cell proliferation.
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