Proteomic analysis of Cry1Ac and Cry2Aa binding proteins in brush border membrane vesicles of the Chilo suppressalis midgut

Qiu, Lin; Wang, Peipei; Zhang, Boyao; Wang, Xiaoping; Lei, Chaoliang; Lin, Yongjun; Ma, Weihua

doi:10.1016/j.aspen.2017.08.025

Cited by 4 publications

(5 citation statements)

References 57 publications

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“…This is reasonable if APN deficiency is lethal to the insect. In contrast, the susceptibility of insect larvae was reduced by downregulation of APN by RNA interference [ 68 , 69 ]. However, further work is required to confirm this, as the downregulation APN was inadequate and the decrease in susceptibility was obscure.…”

Section: Receptor Functions Of Abcc2 Cadherin-like Receptor and mentioning

confidence: 99%

Function and Role of ATP-Binding Cassette Transporters as Receptors for 3D-Cry Toxins

Satō

Adegawa

et al. 2019

Toxins

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When ABC transporter family C2 (ABCC2) and ABC transporter family B1 (ABCB1) were heterologously expressed in non-susceptible cultured cells, the cells swelled in response to Cry1A and Cry3 toxins, respectively. Consistent with the notion that 3D-Cry toxins form cation-permeable pores, Bombyx mori ABCC2 (BmABCC2) facilitated cation-permeable pore formation by Cry1A when expressed in Xenopus oocytes. Furthermore, BmABCC2 had a high binding affinity (KD) to Cry1Aa of 3.1 × 10−10 M. These findings suggest that ABC transporters, including ABCC2 and ABCB1, are functional receptors for 3D-Cry toxins. In addition, the Cry2 toxins most distant from Cry1A toxins on the phylogenetic tree used ABC transporter A2 as a receptor. These data suggest that 3D-Cry toxins use ABC transporters as receptors. In terms of inducing cell swelling, ABCC2 has greater activity than cadherin-like receptor. The pore opening of ABC transporters was hypothesized to be linked to their receptor function, but this was repudiated by experiments using mutants deficient in export activity. The synergistic relationship between ABCC2 and cadherin-like receptor explains their ability to cause resistance in one species of insect.

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Section: Receptor Functions Of Abcc2 Cadherin-like Receptor and mentioning

confidence: 99%

Function and Role of ATP-Binding Cassette Transporters as Receptors for 3D-Cry Toxins

Satō

Adegawa

et al. 2019

Toxins

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“…The binding of the Cry1A toxin to C . suppressalis aminopeptidase (CsAPN) and cadherin (CsCad) expressed in insect cell cultures suggests that these proteins play a role in Cry intoxication 30,31 . The knockdown of two cadherin genes (CsCad1 and CsCad2) reduced the susceptibility of C .…”

Section: Introductionmentioning

confidence: 99%

Cadherin CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in Chilo suppressalis

Chen

Han

et al. 2019

Sci Rep

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Transgenic rice lines expressing Bacillus thuringiensis (Bt) toxins have been successfully developed for the control of Chilo suppressalis . However, the evolution of insect resistance is a major threat to Bt rice durability. Bt toxins function by binding specific receptors in the midgut of target insects; specifically, cadherin proteins have been identified as Cry toxin receptors in diverse lepidopteran species. Here, we report the functional roles of cadherin CsCad in the midgut of C . suppressalis in Cry1Ab and Cry1C toxicity. We expressed a recombinant truncated CsCad peptide (CsCad-CR11-MPED) in Escherichia coli that included the eleventh cadherin repeat and MPED region. Based on ligand blotting and ELISA binding assays, the CsCad-CR11-MPED peptide specifically bound Cry1Ab with high affinity but weakly bound Cry1C. The CsCad-CR11-MPED peptide significantly enhanced the susceptibility of C . suppressalis larvae to Cry1Ab but not Cry1C. Furthermore, the knockdown of endogenous CsCad with Stealth siRNA reduced C . suppressalis larval susceptibility to Cry1Ab but not Cry1C, suggesting that CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in C . suppressalis . This information directly enhances our understanding of the potential resistance mechanisms of C . suppressalis against Bt toxins and may assist in the development of effective strategies for delaying insect resistance.

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“…In B and D, the loading quantities were 0.36, 0.72, and 1.44 μg for lanes 1−3; 1.08 μg for lane 4; 1.5 μg for lane 5 and 6, respectively. suppressalis, 29 Anthonomus grandis, 30 and Ostrinia furnacalis, 31 but they are unlikely to act as a receptor of Cry toxins. 31 It was suggested that Hsps potentially function in protection against Cry intoxication.…”

Section: Resultsmentioning

confidence: 99%

“…These Hsps play roles in an extraordinary variety of normal cellular processes, including protein transport, posttranslational modification, molecular chaperones, and signal transduction . The binding affinity of Hsps with Cry toxins were previously reported in Helicoverpa armigera, Chilo suppressalis, Anthonomus grandis, and Ostrinia furnacalis, but they are unlikely to act as a receptor of Cry toxins . It was suggested that Hsps potentially function in protection against Cry intoxication.…”

Section: Resultsmentioning

confidence: 99%

Evaluation of Cry1Ac and Cry2Aa Toxin Binding to Two Important Beneficial Cotton Field Insects, Harmonia axyridis and Orius similis

Wang

Zhou

et al. 2018

J. Agric. Food Chem.

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Transgenic crops expressing Cry toxins are effective and considered environmentally friendly alternatives to synthetic pesticides, but assessment of environmental risks of their application on nontarget organisms is ongoing. The main risk is the transfer of Cry toxins to natural enemies through the food chain. There is reported evidence supporting that Cry toxins can be detected in the body and gut of some natural enemy insects. Considering that binding of Cry toxins to insect proteins is an essential step in the intoxication process, this work was conducted to evaluate interactions between Cry1Ac and Cry2Aa toxins with proteins from larvae/nymphs and adults of two important predatory natural enemies in cotton fields, Harmonia axyridis and Orius similis. Results support the absence of Cry1Ac or Cry2Aa binding proteins in immature stages of H. axyridis and O. similis, as well as in imaginal stage of H. axyridis. One same binding band about 70 kDa was found in imaginal total protein of O. similis when probed with the two Cry proteins, with the best match to Hsc70 of O. sauteri in the Uniprot database. However, nonspecific binding was verified by following competitive binding assays between the two Cry proteins and imaginal total protein of O. similis. From these results, we may infer that Cry1Ac and Cry2Aa have no likely detrimental effects on H. axyridis and O. similis.

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Proteomic analysis of Cry1Ac and Cry2Aa binding proteins in brush border membrane vesicles of the Chilo suppressalis midgut

Cited by 4 publications

References 57 publications

Function and Role of ATP-Binding Cassette Transporters as Receptors for 3D-Cry Toxins

Function and Role of ATP-Binding Cassette Transporters as Receptors for 3D-Cry Toxins

Cadherin CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in Chilo suppressalis

Evaluation of Cry1Ac and Cry2Aa Toxin Binding to Two Important Beneficial Cotton Field Insects, Harmonia axyridis and Orius similis

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