The Cadherin Protein Is Not Involved in Susceptibility toBacillus thuringiensisCry1Ab or Cry1Fa Toxins inSpodoptera frugiperda

文献类型： 外文期刊

第一作者： Zhang, Jianfeng

作者： Zhang, Jianfeng;Yang, Yanchao;Liu, Leilei;Yang, Yongbo;Liu, Kaiyu;Jin, Minghui;Xiao, Yutao;Gomez, Isabel;Bravo, Alejandra;Soberon, Mario

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关键词： Bacillus thuringiensis; Spodoptera frugiperda; cadherin; Cry1Ab; Cry1Fa; mode of action of Cry toxin

期刊名称：TOXINS （ 影响因子：4.546； 五年影响因子：4.8 ）

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年卷期： 2020 年 12 卷 6 期

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收录情况： SCI

摘要： It is well known that insect larval midgut cadherin protein serves as a receptor ofBacillus thuringiensis(Bt) crystal Cry1Ac or Cry1Ab toxins, since structural mutations and downregulation ofcadgene expression are linked with resistance to Cry1Ac toxin in several lepidopteran insects. However, the role ofSpodoptera frugiperdacadherin protein (SfCad) in the mode of action of Bt toxins remains elusive. Here, we investigated whether SfCad is involved in susceptibility to Cry1Ab or Cry1Fa toxins.In vivo, knockout of theSfCadgene by CRISPR/Cas 9 did not increase tolerance to either of these toxins inS. frugiperdalarvae.In vitrocytotoxicity assays demonstrated that cultured insect TnHi5 cells expressing GFP-tagged SfCad did not increase susceptibility to activated Cry1Ab or Cry1Fa toxins. In contrast, expression of another well recognized Cry1A receptor in this cell line, the ABCC2 transporter, increased the toxicity of both Cry1Ab and Cry1Fa toxins, suggesting that SfABCC2 functions as a receptor of these toxins. Finally, we showed that the toxin-binding region of SfCad did not bind to activated Cry1Ab, Cry1Ac, nor Cry1Fa. All these results support that SfCad is not involved in the mode of action of Cry1Ab or Cry1Fa toxins inS. frugiperda.

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