Purification of an active fragment of Cry1Ie toxin from Bacillus thuringiensis

文献类型： 外文期刊

第一作者： Zhang, Chunlu

作者： Zhang, Chunlu;Lin, Xiaoyin;Zhang, Yanrui;He, Kanglai;Song, Fuping;Zhang, Jie

作者机构：

关键词： Bacillus thuringiensis;Cry1Ie;IE648;Insecticidal activity

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）

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年卷期：

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收录情况： SCI

摘要： The cry1I genes from Bacillus thuringiensis are a class of special genes with unique characteristics; they are silent in B. thuringiensis strains but can be over-expressed in Escherichia coli, resulting in a Cry1I-type protein with a molecular mass of approximately 81 kDa. Cry1I-type protein is toxic to Lepidoptera larvae. A truncated Cry1Ie protein, IE648, which corresponds to the first 648 amino acids from the N-terminus of Cry1Ie, was purified from E. coli using Ni-NTA affinity isolation, Q-Sepharose Fast Flow chromatography, and Superdex-200 size-exclusion chromatography. It was determined using laboratory bioassays that the purified IE648 protein has good insecticidal activity. Heterologous competitive binding assays show that IE648 does not compete with Cry1Ac for binding to the brush border membrane vesicles of the Asian corn borer and does not compete with Cry1Ac at concentrations below a 500-fold excess of unlabeled Cry1Ac for binding to the peritrophic matrix of the insect. This result implies that IE648 may be a good candidate as part of a multiple-toxin strategy for the potential control of resistance in insect pests. The method of purification reported here is valuable for further research on the structure and function of IE648 and in evaluating the biosafety of this protein within transgenic plants.

分类号： Q51

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