Cry toxin mode of action in susceptible and resistant Heliothis virescens larvae
Cry toxin mode of action in susceptible and resistant Heliothis virescens larvae
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DOI：
10.1016/j.jip.2006.01.010
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发表时间：
2006-07-01
影响因子：
3.4
通讯作者：
Adang, Michael J.
中科院分区：
文献类型：
--
作者：
Jurat-Fuentes, Juan Luis;Adang, Michael J.
许多害虫物种通过在植物中递送的苏云金芽孢杆菌（Bt）Cry毒素和生物农药被有效地控制。由于昆虫中肠上皮含有受体和其他决定苏云金杆菌毒性的分子，因此这些分子的表征对于持续使用苏云金杆菌毒素是必要的。通过对烟夜蛾Bt敏感株和抗性株的研究，深入了解了烟夜蛾的抗性机制和毒素受体。例如，在H. Virescens编码钙粘蛋白样蛋白，其是鳞翅目中的功能性Cry1A受体。本文讨论了从H. virescens菌株。我们的研究集中在一个敏感的和三个抗性的H. virescens菌株以鉴定与毒素抗性相关的改变。根据这种方法，我们已经能够确定碱性磷酸酶（HvALP）作为一个潜在的受体，并测试了这种蛋白质作为耐Cry1Ac标记的效用。比较刷状缘蛋白质组从敏感和耐药幼虫，使我们能够确定其他分子直接参与毒性过程。(c)2006年爱思唯尔公司All rights reserved.
Many pest insect species are effectively controlled by Bacillus thuringiensis (Bt) Cry toxins delivered in plants and biopesticides. Since the insect midgut epithelium contains receptors and other molecules that determine Bt toxicity, characterization of these molecules is necessary for sustained usage of Bt toxins. Studies of Bt susceptible and resistant strains of Heliothis virescens have provided insights into resistance mechanisms and toxin receptors. For example, the first gene identified as involved in high levels of Cry1Ac resistance in H. virescens encodes a cadherin-like protein, a functional Cry1A receptor in Lepidoptera. This manuscript discusses the most updated information on the mode of action of Cry1A toxins obtained from the characterization of resistant mechanisms in H. virescens strains. Our studies are focused on biochemical and molecular comparison of a susceptible and three resistant H. virescens strains to identify alterations that correlate with toxin resistance. Following this approach we have been able to identify an alkaline phosphatase (HvALP) as a potential receptor and tested the utility of this protein as a marker for resistance to Cry1Ac. Comparison of brush border proteomes from susceptible and resistant larvae has allowed us to identify additional molecules directly involved in the toxicity process. (c) 2006 Elsevier Inc. All rights reserved.