A protein engineering of Bacillus thuringiensis delta-endotoxin by conjugating with 4 ''-O-succinoyl abamectin

文献类型： 外文期刊

第一作者： Pan, Zhi-Zhen

作者： Pan, Zhi-Zhen;Zhu, Yu-Jing;Chen, Zheng;Ruan, Chuan-Qing;Liu, Bo;Xu, Lian;Chen, Qing-Xi

作者机构：

关键词： BtA;Fluorescence quenching analysis (FQA);Forte-Bio Octet Red System (Forte-Bio ORS)

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2013 年 62 卷

页码：

收录情况： SCI

摘要： Conjugation of Bacillus thuringiensis delta-endotoxin (Bt toxin) with other toxins for insect pest control has been proposed as a new efficient strategy with increasing insecticidal toxicity and target range and delay the onset of insect resistance. A modified method was investigated by conjugating Bt toxin with 4 ''-O-succinoyl abamectin to form a new biocide which was named as BtA. 'Zero-length' cross-linker EDC in combination with NHS activated 4 ''-O-succinoyl abamectin and extended half-life period of active intermediate for binding to Bt toxin. The dissociation constant for 4 ''-O-succinoyl abamectin binding to Bt toxin was 6.44 mu M by fluorescence quenching analysis. BtA showed a higher insecticidal toxicity against Plutella xylostella, while the relative-toxicity multiple of BtA to Bt toxin was calculated as 5.6. The interaction between Bt toxins with their receptors played a key role in toxicity of Bt toxins. The binding analysis showed the dissociation rate for the binding of BtA to its receptors (7.495 x 10(-3) S-1) was twice slower than that of Bt toxin (1.695 x 10(-2) S-1). The relative dissociation constant of BtA to Bt toxin was only 29% for the binding to the receptors. These results demonstrated that BtA bound to the receptor in BBMV with significantly higher affinity compared with Bt toxin. (C) 2013 Elsevier B.V. All rights reserved.

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