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首页> 美国卫生研究院文献>Cytotechnology >Expression of recombinant and mosaic Cry1Ac receptors from Helicoverpa armigera and their influences on the cytotoxicity of activated Cry1Ac to Spodoptera litura Sl-HP cells
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Expression of recombinant and mosaic Cry1Ac receptors from Helicoverpa armigera and their influences on the cytotoxicity of activated Cry1Ac to Spodoptera litura Sl-HP cells

机译：棉铃虫重组和镶嵌Cry1Ac受体的表达及其对活化的Cry1Ac对斜纹夜蛾Shp细胞的细胞毒性的影响

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Bacillus thuringiensis (Bt) toxin receptors play important roles in the killing of pests, and investigation on characterization of the receptors is essential for utilization of Bt and management of insect resistance. Here, recombinant and mosaic receptors of Bt Cry1Ac toxin from Helicoverpa armigera were expressed in Spodoptera litura Sl-HP cells and their influences on cytotoxicity of activated Cry1Ac toxin were investigated. When H. armigera aminopeptidase N1 (APN1), alkaline phosphatase 2 (ALP2) and cadherin fused with or without GFP tag were, respectively, expressed in Sl-HP cells, live cell-immunofluorescence staining detection revealed that the quantity of the toxin binding to cadherin or cadherin-GFP was much more than that binding to ALP2 and APN1 or their fusion proteins with GFP, and only the cadherin- or cadherin-GFP-expressing cells showed aberrant cell morphology after the treatment of the toxin at low concentrations. ALP2 and APN1 fused with or without GFP tag did not significantly enhance the cadherin-mediated cytotoxicity of the toxin. The mosaic ALP-TBR-GFP-GPI was located on cell membrane, but did not bind to the toxin. The mosaic truncated cadherin-GFP-GPI was not located on cell membrane even if the signal peptide was sustained. The concentrations of the toxin resulting in swelling of 50 % cells for noncadherin-expressing Sl-HP cells and cadherin-expressing Hi5 cells were 5.08 and 9.50 µg/ml within 1 h, respectively. Taken together, our data have indicated that the binding affinity of ALP2 and APN1 to activated Cry1Ac toxin is much weaker than that of cadherin and both ALP2 and APN1 do not enhance the cytotoxicity of the toxin even though cadherin is co-expressed, and the mosaic receptor of ALP2 inserted with cadherin toxin binding domain does not mediate cytotoxicity of the toxin. In addition, the noncadherin-expressing Sl-HP cells are more susceptible to activated Cry1Ac than the cadherin-expressing Hi5 cells.
机译：苏云金芽孢杆菌毒素受体在害虫的杀灭中起着重要的作用，对受体特性的研究对于利用Bt和管理抗虫性至关重要。在这里，棉铃虫Bt Cry1Ac毒素的重组和镶嵌受体在斜纹夜蛾Sl-HP细胞中表达，并研究了它们对活化的Cry1Ac毒素的细胞毒性的影响。当棉铃虫氨基肽酶N1（APN1），碱性磷酸酶2（ALP2）和带有或不带有GFP标签的钙黏着蛋白分别在Sl-HP细胞中表达时，活细胞免疫荧光染色检测显示毒素结合到cadherin或cadherin-GFP远远超过了与ALP2和APN1或其与GFP融合蛋白的结合，并且仅在低浓度毒素处理后，表达cadherin或cadherin-GFP的细胞才显示出异常的细胞形态。带有或不带有GFP标签的ALP2和APN1均未显着增强钙粘蛋白介导的毒素的细胞毒性。镶嵌ALP-TBR-GFP-GPI位于细胞膜上，但不与毒素结合。即使信号肽持续存在，镶嵌截短的钙粘蛋白-GFP-GPI也不位于细胞膜上。导致表达非钙粘蛋白的Sl-HP细胞和表达钙粘蛋白的Hi5细胞的50％细胞溶胀的毒素浓度在1小时内分别为5.08和9.50 µg / ml。两者合计，我们的数据表明，ALP2和APN1对活化的Cry1Ac毒素的结合亲和力比钙粘蛋白弱得多，即使Acad2和APN1共同表达钙粘蛋白，并且马赛克，马赛克也不会增强毒素的细胞毒性。插入钙粘蛋白毒素结合域的ALP2受体不会介导毒素的细胞毒性。另外，与表达钙粘蛋白的Hi5细胞相比，非表达钙粘蛋白的Sl-HP细胞对活化的Cry1Ac更敏感。

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