苏云金芽孢杆菌杀虫晶体蛋白的受体及对夜蛾的杀伤作用。

ISRN Microbiology Pub Date : 2013-09-30 eCollection Date: 2013-01-01 DOI:10.1155/2013/940284
Lidia Mariana Fiuza, Neiva Knaak, Rogério Fernando Pires da Silva, João Antônio Pêgas Henriques
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引用次数: 13

摘要

苏云金芽孢杆菌的杀虫晶体蛋白(ICPs)生物测定表明,Cry1Aa、Cry1Ac和Cry1Ba是对芽孢菊幼虫最具活性的毒素。毒素Cry1Da和Cry1Ea毒性较弱,毒素Cry2Aa无活性。利用链霉亲和素介导的检测方法研究了这些ICPs与芽孢单胞虫幼虫中肠部分的结合。观察到的染色模式显示,Cry1Aa和Cry1Ac结合在整个中肠的刷状边缘。然而,Cry1Ba的结合位点在中肠微绒毛中的分布并不均匀。对2龄黄颡鱼幼虫的体内实验证实了体外结合研究的结果。这些结合数据与生物测定结果吻合良好,证明了受体结合与所测ICPs在该昆虫中的毒性之间存在相关性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Receptors and Lethal Effect of Bacillus thuringiensis Insecticidal Crystal Proteins to the Anticarsia gemmatalis (Lepidoptera, Noctuidae).

Receptors and Lethal Effect of Bacillus thuringiensis Insecticidal Crystal Proteins to the Anticarsia gemmatalis (Lepidoptera, Noctuidae).

Receptors and Lethal Effect of Bacillus thuringiensis Insecticidal Crystal Proteins to the Anticarsia gemmatalis (Lepidoptera, Noctuidae).

Bioassays with insecticidal crystal proteins (ICPs) from Bacillus thuringiensis have demonstrated that Cry1Aa, Cry1Ac, and Cry1Ba are the most active toxins on larvae of the Anticarsia gemmatalis. The toxins Cry1Da and Cry1Ea are less toxic, and toxins Cry2Aa are not active. Binding of these ICPs to midgut sections of the A. gemmatalis larvae was studied using streptavidin-mediated detection. The observed staining patterns showed that Cry1Aa and Cry1Ac bound to the brush border throughout the whole length of the midgut. However, the binding sites of Cry1Ba were not evenly distributed in the midgut microvilli. The in vivo assays against larvae of 2nd instar A. gemmatalis confirmed the results from the in vitro binding studies. These binding data correspond well with the bioassay results, demonstrating a correlation between receptors binding and toxicity of the tested ICPs in this insect.

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