苏云金芽孢杆菌 Cry1Ac 毒素与敏感和抗性小菜蛾（Plutella xylostella）氨基肽酶的结合。
Binding of Bacillus thuringiensis Cry1Ac Toxin to Aminopeptidase in Susceptible and Resistant Diamondback Moths (Plutella xylostella).
出版信息
Appl Environ Microbiol. 1997 Mar;63(3):1024-7. doi: 10.1128/aem.63.3.1024-1027.1997.
Abstract
Bacillus thuringiensis Cry1Ac toxin bound to a 120-kDa protein isolated from the brush border membranes of both susceptible and resistant larvae of Plutella xylostella, the diamondback moth. The 120-kDa protein was purified by Cry1Ac toxin affinity chromatography. Like Cry1Ac-binding aminopeptidase N (EC 3.4.11.2) from other insects, this protein was eluted from the affinity column with 200 mM N-acetylgalactosamine. The purified protein had aminopeptidase activity and bound Cry1Ac toxin on ligand blots. Purified aminopeptidase was recognized by antibodies to the cross-reacting determinant found on phosphatidylinositol-specific phospholipase C-solubilized proteins. The results show that the presence of Cry1Ac-binding aminopeptidase in the brush border membrane is not sufficient to confer susceptibility to Cry1Ac. Furthermore, the results do not support the hypothesis that resistance to Cry1Ac was caused by lack of a Cry1Ac-binding aminopeptidase.
摘要
苏云金芽孢杆菌 Cry1Ac 毒素与小菜蛾鳞翅目幼虫的刷状缘膜上的 120kDa 蛋白结合，小菜蛾是小菜蛾的一种。120kDa 蛋白通过 Cry1Ac 毒素亲和层析进行纯化。与其他昆虫的 Cry1Ac 结合氨肽酶 N（EC 3.4.11.2）一样，该蛋白用 200mM N-乙酰半乳糖胺从亲和柱中洗脱。纯化的蛋白具有氨肽酶活性，并在配体印迹上结合 Cry1Ac 毒素。纯化的氨肽酶被针对磷脂酰肌醇特异性磷脂酶 C 溶解蛋白上发现的交叉反应决定簇的抗体识别。结果表明，刷状缘膜中存在 Cry1Ac 结合氨肽酶不足以赋予对 Cry1Ac 的敏感性。此外，结果不支持 Cry1Ac 抗性是由于缺乏 Cry1Ac 结合氨肽酶引起的假设。
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