Fiuza Lidia Mariana, Knaak Neiva, da Silva Rogério Fernando Pires, Henriques João Antônio Pêgas
UNISINOS, Área 2, Laboratório de Microbiologia e Toxicologia, Avenida Unisinos 950, 93022 São Leopoldo, RS, Brazil.
ISRN Microbiol. 2013 Sep 30;2013:940284. doi: 10.1155/2013/940284. eCollection 2013.
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.
苏云金芽孢杆菌杀虫晶体蛋白(ICP)的生物测定表明,Cry1Aa、Cry1Ac和Cry1Ba是对豆毒蛾幼虫活性最强的毒素。Cry1Da和Cry1Ea毒素毒性较小,而Cry2Aa毒素无活性。利用链霉亲和素介导的检测方法研究了这些ICP与豆毒蛾幼虫中肠切片的结合情况。观察到的染色模式表明,Cry1Aa和Cry1Ac在整个中肠长度上均与刷状缘结合。然而,Cry1Ba的结合位点在中肠微绒毛中分布不均。对二龄豆毒蛾幼虫的体内试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非常吻合,表明在这种昆虫中,受体结合与受试ICP的毒性之间存在相关性。