Biologically active human bone morphogenetic protein 4 fused to collagen-binding domain produced in silkworm-baculovirus expression system

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  • Imai Saki
    Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
  • Li Zhiqing
    Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
  • Iiyama Kazuhiro
    Laboratory of Insect Pathology, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
  • Miyagawa Yoshitaka
    National Research Institute for Child Health and Development
  • Toyoda Masashi
    National Research Institute for Child Health and Development
  • Umezawa Akihiro
    National Research Institute for Child Health and Development
  • Mon Hiroaki
    Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
  • Kusakabe Takahiro
    Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
  • Yoshimura Kaito
    Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences
  • Man Lee Jae
    Laboratory of Silkworm Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences

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Description

Human bone morphogenetic protein 4 (BMP4) fused to the collagen-binding domain (CBD) of fibronectin was constructed and expressed in a silkworm-baculovirus expression system. When recombinant BmNPV was injected into the silkworm larvae and harvested after approximately 4 days, 0.22mg/ml (0.1mg/larva) of recombinant CBD-BMP4 was secreted into the silkworm haemolymph. Interestingly, cultured silkworm cells infected with the same recombinant virus could not secrete the recombinant CBD-BMP4 into culture media. The purified rCBD-BMP4 showed Smad- and MAPK-stimulating activities in human UET-13 cells.<br>

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