苏云金芽孢杆菌 Cry1Ab 毒素在褐飞虱，Nilaparvata lugens（Stål）中的蛋白水解加工。
Proteolytic processing of Bacillus thuringiensis toxin Cry1Ab in rice brown planthopper, Nilaparvata lugens (Stål).
机构信息
Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, Fujian Agriculture and Forestry University, 350002 Fuzhou, Fujian, PR China.
出版信息
J Invertebr Pathol. 2013 Nov;114(3):255-7. doi: 10.1016/j.jip.2013.09.001. Epub 2013 Sep 8.
To understand the low toxicity of Cry toxins in planthoppers, proteolytic activation of Cry1Ab in Nilaparvata lugens was studied. The proteolytic processing of Cry1Ab protoxin by N. lugens midgut proteases was similar to that by trypsin activated Cry1Ab. The Cry1Ab processed with N. lugens midgut proteases was highly insecticidal against Plutella xylostella. However, Cry1Ab activated either by trypsin or the gut proteases of the brown planthopper showed low toxicity in N. lugens. Binding analysis showed that activated Cry1Ab bound to brush border membrane vesicles (BBMV) from N. lugens at a significantly lower level than to BBMV from P. xylostella.
为了理解 Cry 毒素在叶蝉中的低毒性，研究了 Nilaparvata lugens 中 Cry1Ab 的蛋白水解激活。Cry1Ab 原毒素被 N. lugens 中肠蛋白酶的蛋白水解加工过程与胰蛋白酶激活的 Cry1Ab 相似。用 N. lugens 中肠蛋白酶处理的 Cry1Ab 对小菜蛾具有高度的杀虫活性。然而，用胰蛋白酶或褐飞虱中肠蛋白酶激活的 Cry1Ab 在 N. lugens 中表现出低毒性。结合分析表明，与小菜蛾的 BBMV 相比，激活的 Cry1Ab 与 N. lugens 的刷状缘膜囊泡 (BBMV) 的结合水平显著降低。
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