Expression of Cry1Ac toxin-binding region in Plutella xyllostella cadherin-like receptor and studying their interaction mode by molecular docking and site-directed mutagenesis

Hu, Xiaodan; Zhang, Xiao; Zhong, Jianfeng; Liu, Yuan; Zhang, Cunzheng; Xie, Yajing; Lin, Manman; Xu, Chongxin; Lü, Lei; Zhu, Qing; Liu, Xianjin

doi:10.1016/j.ijbiomac.2017.12.135

Cited by 14 publications

(21 citation statements)

References 45 publications

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“…As mentioned above, S. frugiperda ABCC2 mutations are linked with resistance to Cry1Fa [27,28,31]. Interestingly, some Cry1Fa-resistant S. frugiperda strains showed cross-resistance to Cry1Ab or Cry1Ac toxins but not to Cry2Ab or Vip3Aa toxins [20,23]. In the present study, the knockout and over-expression of the SfCad gene revealed that SfCad is not involved in susceptibility of S. frugiperda to Cry1Ab, Cry1Fa, nor Vip3Aa toxins.…”

Section: Discussionsupporting

confidence: 52%

“…For instance, it has been reported that the cadherin from Plutella xylostella (PxCad) is not associated with resistance in P. xylostella to Cry1Ac [17]. However, other reports suggest that PxCad is a functional receptor of Cry1Ac, since PxCad can increase cytotoxicity of Cry1Ac when expressed in the Sf9 cell line [18][19][20]. In addition, we reported that Spodoptera litura cadherin (SlCad), in contrast to HaCad, cannot increase cytotoxicity of Cry1Ac when expressed in Hi5 cells, suggesting that SlCad is not a functional receptor of Cry1Ac in S. litura [14].…”

Section: Introductionmentioning

confidence: 99%

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The Cadherin Protein Is Not Involved in Susceptibility to Bacillus thuringiensis Cry1Ab or Cry1Fa Toxins in Spodoptera frugiperda

Zhang

Jin

Yang

et al. 2020

Toxins

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It is well known that insect larval midgut cadherin protein serves as a receptor of Bacillus thuringiensis (Bt) crystal Cry1Ac or Cry1Ab toxins, since structural mutations and downregulation of cad gene expression are linked with resistance to Cry1Ac toxin in several lepidopteran insects. However, the role of Spodoptera frugiperda cadherin 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 the SfCad gene by CRISPR/Cas 9 did not increase tolerance to either of these toxins in S. frugiperda larvae. In vitro cytotoxicity 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 in S. frugiperda.

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Section: Discussionsupporting

confidence: 52%

Section: Introductionmentioning

confidence: 99%

The Cadherin Protein Is Not Involved in Susceptibility to Bacillus thuringiensis Cry1Ab or Cry1Fa Toxins in Spodoptera frugiperda

Zhang

Jin

Yang

et al. 2020

Toxins

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“…Since CADs were first identified as Cry toxin binding proteins in Manduca sexta (Vadlamudi et al ., ), a substantial number of studies have demonstrated that cadherin is a receptor of Cry toxins in lepidopteran, coleopteran and dipteran insects (Morin et al ., ; Flannagan et al ., ; Hua et al ., ; Park et al ., ; Gong et al ., ; Qiu et al ., ; Ren et al ., ; Wang et al ., ; Hu et al ., ). Our present study revealed two CAD isoforms, CsCAD3 and CsCAD4 , from the transcriptome of C. suppressalis .…”

Section: Discussionmentioning

confidence: 97%

Knockdown of cadherin genes decreases susceptibility of Chilo suppressalis larvae to Bacillus thuringiensis produced Crystal toxins

Zhou

Huang

et al. 2020

Insect Molecular Biology

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The striped rice stem borer, Chilo suppressalis Walker, is one of the most destructive rice pests in Asia. Insecticidal crystal proteins (Cry toxins) produced by Bacillus thuringiensis are widely used as biopesticides or in developing transgenic crops for pest management. In this study, we tested the involvement of two newly cloned C. suppressalis cadherins (CsCAD3 and CsCAD4) in the toxicity of Cry1Ab/Ac, Cry2Aa and Cry1Ca. Our results showed that CsCAD4 was expressed highest in the midgut, whereas CsCAD3 was expressed highest in the epidermis. The feeding of double-stranded RNA specific to CsCAD3 and CsCAD4 respectively significantly suppressed the expressions of target gene. The knockdown of CsCAD3 significantly reduced the mortality of larvae to Cry1Ab/Ac, whereas knockdown of CsCAD4 significantly decreased the larval susceptibility to Cry2Aa. In contrast, reduced expressions of CsCAD3 or CsCAD4 were not interacted with larval susceptibility to Cry1Ca. Our results suggest that CsCAD3 and CsCAD4 function in Cry toxin toxicity and these findings will help us to better understand the action mechanism of Cry toxins in C. suppressalis.

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“…It is well known that the interaction between Cry toxin and toxin receptors from the host midgut brush border membrane vesicles (BBMVs) is the initial step in the insecticidal activity of the Cry protein toxins [ 107 , 108 , 109 , 110 ]. Several researchers also showed the interaction between midgut immune-related proteins and Cry toxin [ 111 , 112 , 113 ].…”

Section: The Host Immune System In Response To Bt Infectionmentioning

confidence: 99%

The Tripartite Interaction of Host Immunity–Bacillus thuringiensis Infection–Gut Microbiota

Mandal

et al. 2020

Toxins

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Bacillus thuringiensis (Bt) is an important cosmopolitan bacterial entomopathogen, which produces various protein toxins that have been expressed in transgenic crops. The evolved molecular interaction between the insect immune system and gut microbiota is changed during the Bt infection process. The host immune response, such as the expression of induced antimicrobial peptides (AMPs), the melanization response, and the production of reactive oxygen species (ROS), varies with different doses of Bt infection. Moreover, B. thuringiensis infection changes the abundance and structural composition of the intestinal bacteria community. The activated immune response, together with dysbiosis of the gut microbiota, also has an important effect on Bt pathogenicity and insect resistance to Bt. In this review, we attempt to clarify this tripartite interaction of host immunity, Bt infection, and gut microbiota, especially the important role of key immune regulators and symbiotic bacteria in the Bt killing activity. Increasing the effectiveness of biocontrol agents by interfering with insect resistance and controlling symbiotic bacteria can be important steps for the successful application of microbial biopesticides.

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Expression of Cry1Ac toxin-binding region in Plutella xyllostella cadherin-like receptor and studying their interaction mode by molecular docking and site-directed mutagenesis

Cited by 14 publications

References 45 publications

The Cadherin Protein Is Not Involved in Susceptibility to Bacillus thuringiensis Cry1Ab or Cry1Fa Toxins in Spodoptera frugiperda

The Cadherin Protein Is Not Involved in Susceptibility to Bacillus thuringiensis Cry1Ab or Cry1Fa Toxins in Spodoptera frugiperda

Knockdown of cadherin genes decreases susceptibility of Chilo suppressalis larvae to Bacillus thuringiensis produced Crystal toxins

The Tripartite Interaction of Host Immunity–Bacillus thuringiensis Infection–Gut Microbiota

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