College of Life Science, Hunan Provincial Key Laboratory of Microbial Molecular Biology-State Key Laboratory Breeding Base of Microbial Molecular Biology, Hunan Normal University, Changsha, 410081, China.
World J Microbiol Biotechnol. 2012 Jan;28(1):397-400. doi: 10.1007/s11274-011-0825-0. Epub 2011 Jun 24.
In order to provide guidance for selecting suitable heterogenous gene that can efficiently enhance toxicity or broaden insecticidal spectrum of Cry1Ac through fusion expression, two hybrid cry1Acs fused with chitinase-encoding gene tchiB and neurotoxin gene hwtx-1 respectively were constructed and their toxicities were compared. A Bacillus thuringiensis strain harboring the cry1Ac gene in vector pHT315 was used as control. Bioassay revealed that LC(50) (after 72 h) of Cry1Ac protoxin was 41.01 μg mL(-1), while the hybrid cry1Acs fused with tchiB and hwtx-1 were 4.89 and 23.14 μg mL(-1), which were 8.23- and 1.77-fold higher than Cry1Ac protoxin in terms of relative toxicity respectively. Both fusion crystals had a higher toxicity than the original Cry1Ac protein and the toxicity of hybrid cry1Acs fused with hwtx-1 experienced a more significant increase than that fused with tchiB.
为了通过融合表达筛选出能够有效提高毒力或拓宽杀虫谱的合适异源基因，构建了两种分别与几丁质酶编码基因 tchiB 和神经毒素基因 hwtx-1 融合的杂交 cry1Acs，并比较了它们的毒性。以含有载体 pHT315 中 cry1Ac 基因的苏云金芽孢杆菌菌株为对照。生物测定显示，Cry1Ac 原毒素的 LC50（72 小时后）为 41.01 μg mL-1，而与 tchiB 和 hwtx-1 融合的杂交 cry1Acs 分别为 4.89 和 23.14 μg mL-1，相对毒性分别比 Cry1Ac 原毒素高 8.23 倍和 1.77 倍。两种融合晶体的毒性均高于原始 Cry1Ac 蛋白，与 tchiB 融合的杂交 cry1Acs 的毒性比与 hwtx-1 融合的毒性增加更为显著。
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