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

作　　者：GUO Shu-yuan LI Jie CHEN Zhen HE Kang-lai 

机构地区：[1]School of Life Science,Beijing Institute of Technology [2]State Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences

出　　处：《Journal of Integrative Agriculture》2014年第5期1043-1050,共8页农业科学学报（英文版）

基　　金：funded by the National 973 Program of China (2009CB118902);the Natinoal Natural Science Foundation of China (31171911)

摘　　要：Domain I of the activated Crystal protein from Bacillus thuringiensis has a seven a-helix bundle structure, which is responsible for membrane channel formation in its insecticidal mechanism. Crylle is toxic to Asian corn borer, Ostrinia furnacalis （Guen6e）, and plays important roles in insect biological control. The domain I from Crylle 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 Crylle-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 Crylle-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.Domain I of the activated Crystal protein from Bacillus thuringiensis has a seven a-helix bundle structure, which is responsible for membrane channel formation in its insecticidal mechanism. Crylle is toxic to Asian corn borer, Ostrinia furnacalis （Guen6e）, and plays important roles in insect biological control. The domain I from Crylle 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 Crylle-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 Crylle-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 Cryl Ie domain I of Cry protein monolayer insertion 

分 类 号：S476.1[农业科学—农业昆虫与害虫防治]