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SfABCC2 transporter extracellular loops 2 and 4 are responsible for the Cry1Fa insecticidal specificity against Spodoptera frugiperda

文献类型： 外文期刊

作者： Liu, Yuanyuan 1 ; Jin, Minghui 2 ; Wang, Ling 3 ; Wang, Haixia 1 ; Xia, Zhichao 1 ; Yang, Yongbo 1 ; Bravo, Alejandra; 1 ;

作者机构： 1.Cent China Normal Univ, Sch Life Sci, Inst Entomol, Wuhan 430079, Peoples R China

2.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Shenzhen 518120, Peoples R China

3.Hubei Acad Agr Sci, Inst Plant Protect & Soil Fertil, Minist Agr,Hubei Key Lab Crop Dis Insect Pests &, Key Lab Integrated Pest Management Crops Cent Chi, Wuhan 430064, Peoples R China

4.Univ Nacl Autonoma Mexico, Inst Biotecnol, Apdo Postal 510-3, Cuernavaca 62250, Morelos, Mexico

关键词： ABCC2; Cry1Fa; Cry1Ab; Bacillus thuringiensis; Spodoptera frugiperda; Mythimna separata

期刊名称：INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY （ 影响因子：4.714； 五年影响因子：4.953 ）

ISSN： 0965-1748

年卷期： 2021 年 135 卷

页码：

收录情况： SCI

摘要： Bacillus thuringiensis (Bt) bacteria produce Cry toxins that kill insect pests. Insect specificity of Cry toxins relies on their binding to larval gut membrane proteins such as cadherin and ATP-binding cassette (ABC) transporter proteins. Mutations in ABC transporters have been implicated in high levels of resistance to Cry toxins in multiple pests. Spodoptera frugiperda is an insect pest susceptible to Cry1Fa and Cry1Ab toxins while Mythimna separata is tolerant to Cry1Fa and less susceptible to Cry1Ab. Here, we analyzed the potential role of ABCC2 in determining the susceptibility of S. frugiperda to Cry1Fa and Cry1Ab, by expressing SfABCC2 or MsABCC2 in Hi5 insect cell line and by the systematic replacements of extracellular loops (ECLs) between these two proteins. Expression of SfABCC2 in Hi5 conferred susceptibility to both Cry1Fa and Cry1Ab, in contrast to the expression of MsABCC2 that mediated low toxicity to Cry1Ab and no toxicity to Cry1Fa in agreement with their larvicidal toxicities. The SfABCC2 and MsABCC2 amino acid sequences showed differential residues among ECL1, ECL2, ECL4 and ECL6 loops, while ECL3 and ECL5 share the same primary sequence. The exchange of ECLs between SfABCC2 and MsABCC2 demonstrated that ECL4 and ECL2 contribute to Cry1Fa toxicity, where ECL4 plays a major role. The medium region (named M2) of ECL4 was identified as the most important region of SfABCC2 involved in Cry1Fa toxicity as shown by point mutations in this region. These findings will be helpful to understand the mechanisms of action of Bt toxins in S. frugiperda.

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