Production of biologically active human interferon-α in transgenic rice

DOI Web Site 被引用文献2件 参考文献63件
  • Masumura Takehiro
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University
  • Morita Satoshi
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University
  • Miki Yoshiyuki
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University
  • Kurita Akihiro
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University
  • Morita Shigeto
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University
  • Shirono Hiroyuki
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University Laboratories for Bioengineering and Research, Research Division, JCR Pharmaceuticals Co., Ltd.
  • Koga Junichi
    Laboratories for Bioengineering and Research, Research Division, JCR Pharmaceuticals Co., Ltd.
  • Tanaka Kunisuke
    Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University

書誌事項

タイトル別名
  • Production of biologically active human interferon-.ALPHA. in transgenic rice
  • Production of biologically active human interferon アルファ in transgenic rice

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抄録

Interferon-α (IFN-α) is a principle cytokine that plays a key regulatory role in mammalian immune systems. The recombinant DNA of IFN-α is composed of the signal sequence region for rice 10 kDa prolamin cDNA, the amino-terminal region of β-glucuronidase DNA, and the mature polypeptide region of human IFN-αDNA, and is expected to produce a biologically active form of IFN-α. This chimerical DNA for coding IFN-α under the control of a cauliflower mosaic virus 35S promoter and a 5′-intron of rice cytosolic superoxide dismutase gene (sodcC1), was transformed into dwarf rice by an Agrobacterium-mediated system. Three lines of transgenic rice plant expressing various levels of IFN-α polypeptide were finally generated. The expression level of the recombinant polypeptide in each line was analyzed by an IFN-α antiviral activity assay and enzyme immunoassay. Higher expression of IFN-α was achieved in developing seed endosperm in two of transgenic rice lines. The replacement of the native signal peptide of IFN-α with the prolamin signal peptide was effective for transporting the IFN-α polypeptide into the ER-derived protein body of developing seed endosperm. These results suggest that rice can be used to produce many biologically active mammalian proteins that accumulate in target organelles such as protein bodies.

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