Journal of Integrative Agriculture ›› 2014, Vol. 13 ›› Issue (5): 1043-1050.DOI: 10.1016/S2095-3119(13)60589-4

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Penetration of a Single Domain of Bacillus thuringiensis Cry1Ie-Domain I to a Lipid Membrane In vitro

 GUO Shu-yuan, LI Jie, CHEN Zhen , HE Kang-lai   

  1. 1、School of Life Science, Beijing Institute of Technology, Beijing 100081, P.R.China
    2、State Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences,
    Beijing 100193, P.R.China
  • 收稿日期:2013-03-20 出版日期:2014-05-01 发布日期:2014-05-06
  • 通讯作者: GUO Shu-yuan, Tel: +86-10-68914495, E-mail: guosy@bit.edu.cn
  • 基金资助:

    This work was funded by the National 973 Program of China (2009CB118902), the Natinoal Natural Science Foundation of China (31171911). We thank Professor Sui Sengfang from the Department of Biological Science and Biotechnology, Tsinghua University, for providing the NIMA 9000 microbalance.

Penetration of a Single Domain of Bacillus thuringiensis Cry1Ie-Domain I to a Lipid Membrane In vitro

 GUO Shu-yuan, LI Jie, CHEN Zhen , HE Kang-lai   

  1. 1、School of Life Science, Beijing Institute of Technology, Beijing 100081, P.R.China
    2、State Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences,
    Beijing 100193, P.R.China
  • Received:2013-03-20 Online:2014-05-01 Published:2014-05-06
  • Contact: GUO Shu-yuan, Tel: +86-10-68914495, E-mail: guosy@bit.edu.cn
  • Supported by:

    This work was funded by the National 973 Program of China (2009CB118902), the Natinoal Natural Science Foundation of China (31171911). We thank Professor Sui Sengfang from the Department of Biological Science and Biotechnology, Tsinghua University, for providing the NIMA 9000 microbalance.

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摘要： Domain I of the activated Crystal protein from Bacillus thuringiensis has a seven α-helix bundle structure, which is responsible for membrane channel formation in its insecticidal mechanism. Cry1Ie is toxic to Asian corn borer, Ostrinia furnacalis (Guenée), and plays important roles in insect biological control. The domain I from Cry1Ie has been expressed and purified in its normal conformation, as embedded in the full length homologous toxin structure. The membrane insertion ability of this single domain was compared with the full length homologous toxin using a monolayer insertion experiment. The results indicated that the Cry1Ie-domain I had the ability to insert into the lipid monolayer, and this ability is greater than that of the IE648 toxin. However, the state of insertion is not stable and remains for only a short period of time. The Cry1Ie-domain I plays no role in receptor binding as it had a nonspecific binding with the brush border membrane vesicles of the Asian corn borer.

关键词: Bacillus thuringiensis , Cry1Ie , domain I of Cry protein , monolayer insertion

Abstract: Domain I of the activated Crystal protein from Bacillus thuringiensis has a seven α-helix bundle structure, which is responsible for membrane channel formation in its insecticidal mechanism. Cry1Ie is toxic to Asian corn borer, Ostrinia furnacalis (Guenée), and plays important roles in insect biological control. The domain I from Cry1Ie has been expressed and purified in its normal conformation, as embedded in the full length homologous toxin structure. The membrane insertion ability of this single domain was compared with the full length homologous toxin using a monolayer insertion experiment. The results indicated that the Cry1Ie-domain I had the ability to insert into the lipid monolayer, and this ability is greater than that of the IE648 toxin. However, the state of insertion is not stable and remains for only a short period of time. The Cry1Ie-domain I plays no role in receptor binding as it had a nonspecific binding with the brush border membrane vesicles of the Asian corn borer.

Key words: Bacillus thuringiensis , Cry1Ie , domain I of Cry protein , monolayer insertion