A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resistance to Cry1Ab

Xu, Lei; Ferry, Nicolas; Wang, Zhenying; Zhang, Jie; Edwards, Martin G.; Gatehouse, Angharad M. R.; He, Kanglai

doi:10.1007/s11248-013-9718-3

Cited by 32 publications

(30 citation statements)

References 59 publications

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“…It was found that a transgenic maize line expressing cry1Ie was highly resistant against the stem borer O. furnacalis [24]. In addition, it appears that the Cry1Ie protein has no cross-resistance with other Lepidoptera-active insecticidal proteins such as Cry1Ab, Cry1Ac, Cry1Ah, or Cry1F [25,26,27], making it a suitable candidate gene for developing stacked events for improved pest control. However, our knowledge regarding the potential effects of the Cry1Ie protein on non-target beneficial arthropods is still limited.…”

Section: Discussionmentioning

confidence: 99%

Consumption of Bt Maize Pollen Containing Cry1Ie Does Not Negatively Affect Propylea japonica (Thunberg) (Coleoptera: Coccinellidae)

Liu

et al. 2017

Toxins

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Propylea japonica (Thunberg) (Coleoptera: Coccinellidae) are prevalent predators and pollen feeders in East Asian maize fields. They are therefore indirectly (via prey) and directly (via pollen) exposed to Cry proteins within Bt-transgenic maize fields. The effects of Cry1Ie-producing transgenic maize pollen on the fitness of P. japonica was assessed using two dietary-exposure experiments in the laboratory. In the first experiment, survival, larval developmental time, adult fresh weight, and fecundity did not differ between ladybirds consuming Bt or non-Bt maize pollen. In the second experiment, none of the tested lethal and sublethal parameters of P. japonica were negatively affected when fed a rapeseed pollen-based diet containing Cry1Ie protein at 200 μg/g dry weight of diet. In contrast, the larval developmental time, adult fresh weight, and fecundity of P. japonica were significantly adversely affected when fed diet containing the positive control compound E-64. In both experiments, the bioactivity of the Cry1Ie protein in the food sources was confirmed by bioassays with a Cry1Ie-sensitive lepidopteran species. These results indicated that P. japonica are not affected by the consumption of Cry1Ie-expressing maize pollen and are not sensitive to the Cry1Ie protein, suggesting that the growing of Bt maize expressing Cry1Ie protein will pose a negligible risk to P. japonica.

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Section: Discussionmentioning

confidence: 99%

Consumption of Bt Maize Pollen Containing Cry1Ie Does Not Negatively Affect Propylea japonica (Thunberg) (Coleoptera: Coccinellidae)

Liu

et al. 2017

Toxins

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“…Understanding the mode of action underlying Cry toxin interactions with their hosts is critical for elucidating the molecular basis of toxin specificity and facilitating the development of new pest management tools. V‐ATPase has been identified as a Cry toxin‐binding protein in Heliothis virescens (Cry1Ac), Helicoverpa armigera (Cry1Ac) and Ostrinia furnacalis (Cry1Ab) (Krishnamoorthy et al ., ; Chen et al ., ; Xu et al ., ). Our previous studies suggest that V‐ATPase subunits A and B are Cry2Aa toxin‐binding proteins in Spodoptera exigua (Qiu et al ., ).…”

Section: Discussionmentioning

confidence: 97%

“…V‐ATPases are located in the goblet cell apical membrane, which is involved in energy production and conversion (Nishi and Forgac, ; Beyenbach and Wieczorek, ). Evidence from a number of studies appears to indicate a role for V‐ATPase in the toxicity of Cry proteins in susceptible insects (Krishnamoorthy et al ., ; Chen et al ., ; Nakasu et al ., ; Contreras et al ., ; Xu et al ., ; Zhou et al ., ). The potential role of the V‐ATPase subunit A in mediating the toxicity of Bt Cry toxins in C. suppressalis has not previously been examined.…”

Section: Introductionmentioning

confidence: 99%

The midgut V‐ATPase subunit A gene is associated with toxicity to crystal 2Aa and crystal 1Ca‐expressing transgenic rice in Chilo suppressalis

Qiu

Sun

Jiang

et al. 2019

Insect Molecular Biology

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Insecticidal crystal (Cry) proteins produced by the bacterium Bacillus thuringiensis (Bt) are toxic to a diverse range of insects. Transgenic rice expressing Cry1A, Cry2A and Cry1C toxins have been developed that are lethal to Chilo suppressalis, a devastating insect pest of rice in China. Identifying the mechanisms underlying the interactions of Cry toxins with susceptible hosts will improve both our understanding of Cry protein toxicology and long‐term efficacy of Bt crops. In this study, we tested the hypothesis that V‐ATPase subunit A contributes to the action of Cry1Ab/1Ac, Cry2Aa and Cry1Ca toxins in C. suppressalis. The full‐length V‐ATPase subunit A transcript was initially cloned from the C. suppressalis larval midgut and then used to generate double‐stranded RNA (dsRNA)‐producing bacteria. Toxicity assays using transgenic rice lines TT51 (Cry1Ab and Cry1Ac fusion genes), T2A‐1 (Cry2Aa), and T1C‐19 (Cry1Ca) in conjunction with V‐ATPase subunit A dsRNA‐treated C. suppressalis larvae revealed significantly reduced larval susceptibility to T2A‐1 and T1C‐19 transgenic rice, but not to TT51 rice. These results suggest that the V‐ATPase subunit A plays a crucial role in mediating Cry2Aa and Cry1Ca toxicity in C. suppressalis. These findings will have significant implications on the development of future resistance management tools.

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“…V-ATPase up-regulation has been found to be related to Cry1Ac resistance in Plodia interpunctella and P. xylostella 3031. Although V-ATPase has been identified as a Cry toxin-binding protein in H. virescens (Cry1Ac), H. armigera (Cry1Ac) and O. furnacalis (Cry1Ab)323334, little is known about its function with regard to Cry toxins in other insects. Interestingly, RNA silencing of the A. aegypti ATP synthase subunit beta increased larval mortality to Cry toxins, which suggests that this protein is involved in Cry toxin resistance35.…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of Cry2Aa-binding proteins and their receptor function in Spodoptera exigua

Qiu

Zhang

et al. 2017

Sci Rep

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The bacterium Bacillus thuringiensis produces Crystal (Cry) proteins that are toxic to a diverse range of insects. Transgenic crops that produce Bt Cry proteins are grown worldwide because of their improved resistance to insect pests. Although Bt “pyramid” cotton that produces both Cry1A and Cry2A is predicted to be more resistant to several lepidopteran pests, including Spodoptera exigua, than plants that produce Cry1Ac alone, the mechanisms responsible for the toxicity of Cry2Aa in S. exigua are not well understood. We identified several proteins that bind Cry2Aa (polycalin, V-ATPase subunits A and B, actin, 4-hydroxybutyrate CoA-transferase [4-HB-CoAT]), and a receptor for activated protein kinase C (Rack), in S. exigua. Recombinant, expressed versions of these proteins were able to bind the Cry2Aa toxin in vitro assays. RNA interference gene knockdown of the Se-V-ATPase subunit B significantly decreased the susceptibility of S. exigua larvae to Cry2Aa, whereas knockdown of the other putative binding proteins did not. Moreover, an in vitro homologous competition assay demonstrated that the Se-V-ATPase subunit B binds specifically to the Cry2Aa toxin, suggesting that this protein acts as a functional receptor of Cry2Aa in S. exigua. This the first Cry2Aa toxin receptor identified in S. exigua brush-border membrane vesicles.

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A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resistance to Cry1Ab

Cited by 32 publications

References 59 publications

Consumption of Bt Maize Pollen Containing Cry1Ie Does Not Negatively Affect Propylea japonica (Thunberg) (Coleoptera: Coccinellidae)

Consumption of Bt Maize Pollen Containing Cry1Ie Does Not Negatively Affect Propylea japonica (Thunberg) (Coleoptera: Coccinellidae)

The midgut V‐ATPase subunit A gene is associated with toxicity to crystal 2Aa and crystal 1Ca‐expressing transgenic rice in Chilo suppressalis

Proteomic analysis of Cry2Aa-binding proteins and their receptor function in Spodoptera exigua

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