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将化学合成的蜘蛛毒素蛋白酶抑制剂基因hwtx-11克隆至载体pGEX4T-1上,在大肠杆菌BL21(DE3)中进行表达.重组菌株在IPTG诱导下,经SDS-PAGE和Western blot分析表明,表达的GST-HWTX-11融合蛋白的相对分子量约为33 kD.对重组菌株诱导表达后的产物进行生物活性测定,GST-HWTX-11融合蛋白对甜菜夜蛾(Spodoptera exiguaHubner)和棉铃虫(Helicoverpa armigera)在3d时的LC50分别为86.6μg/mL、119.4μg/mL;其与Cry1Ac对甜菜夜蛾和棉铃虫幼虫毒力也有明显的协同作用.
The chemically synthesized spider toxin protease inhibitor hwtx-11 was cloned into vector pGEX4T-1 and expressed in E.coli BL21 (DE3) .The recombinant strain was induced by IPTG and analyzed by SDS-PAGE and Western blot The relative molecular weight of the GST-HWTX-11 fusion protein was about 33 kD.The biological activity of the recombinant strain after induction of expression was determined. The effect of the GST-HWTX-11 fusion protein on Spodoptera exigua Hubner and Helicoverpa armigera ) Had LC50 of 86.6μg / mL and 119.4μg / mL at 3d, respectively, which showed synergistic effect with Cry1Ac on the toxicity of beet armyworm and cotton bollworm larvae.