Expressing a moth abcc2 gene in transgenic Drosophila causes susceptibility to Bt Cry1Ac without requiring a cadherin-like protein receptor

Stevens, Tristan; Song, Siyu; Bruning, John B.; Choo, Amanda; Baxter, Simon W.

doi:10.1016/j.ibmb.2016.11.008

Cited by 49 publications

(39 citation statements)

References 49 publications

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“…Several primary and secondary types of toxin receptors have been identified in the Lepidoptera and Diptera mosquitoes such as cadherin-like proteins, aminopeptidases, GPI-anchored alkaline phosphatases 8 , and more recently the ATP dependent binding cassette reporter C2 52 . No orthologues of the Lepidoptera cadherin-like Cry receptors were found in Drosophila 52 , supporting the idea of the lack of effect of Btk toxins on these flies. Yet, Drosophila flies may have other types of Cry receptors, therefore explaining the developmental impacts observed, but this remains to be investigated.…”

Section: Discussionmentioning

confidence: 99%

Differential side-effects of Bacillus thuringiensis bioinsecticide on non-target Drosophila flies

Babin

Nawrot-Esposito

Gallet

et al. 2020

Sci Rep

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Bioinsecticides based on Bacillus thuringiensis (Bt) spores and toxins are increasingly popular alternative solutions to control insect pests, with potential impact of their accumulation in the environment on non-target organisms. Here, we tested the effects of chronic exposure to commercial Bt formulations (Bt var. kurstaki and israelensis) on eight non-target Drosophila species present in Bt-treated areas, including D. melanogaster (four strains). Doses up to those recommended for field application (~ 106 Colony Forming Unit (CFU)/g fly medium) did not impact fly development, while no fly emerged at ≥ 1000-fold this dose. Doses between 10- to 100-fold the recommended one increased developmental time and decreased adult emergence rates in a dose-dependent manner, with species-and strain-specific effect amplitudes. Focusing on D. melanogaster, development alterations were due to instar-dependent larval mortality, and the longevity and offspring number of adult flies exposed to bioinsecticide throughout their development were moderately influenced. Our data also suggest a synergy between the formulation compounds (spores, cleaved toxins, additives) might induce the bioinsecticide effects on larval development. Although recommended doses had no impact on non-target Drosophila species, misuse or local environmental accumulation of Bt bioinsecticides could have side-effects on fly populations with potential implications for their associated communities.

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Section: Discussionmentioning

confidence: 99%

Differential side-effects of Bacillus thuringiensis bioinsecticide on non-target Drosophila flies

Babin

Nawrot-Esposito

Gallet

et al. 2020

Sci Rep

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“…It is still not known how ABCA2 is involved in the susceptibility of larvae to Cry2A toxins. ABCA2 is a membrane protein and the ABC transporter ABCC2 is a functional Cry1A toxin receptor [5,16,18,24,25]. Therefore, we examined whether BmABCA2 transiently expressed in HEK293T cells ( Figure 5) could function as a Cry2Ab receptor and whether HEK293T cells would swell like the columnar cells in a Cry toxin-intoxicated midgut.…”

Section: Discussionmentioning

confidence: 99%

ATP-Binding Cassette Subfamily a Member 2 Is a Functional Receptor for Bacillus thuringiensis Cry2A Toxins in Bombyx mori, But Not for Cry1A, Cry1C, Cry1D, Cry1F, or Cry9A Toxins

Miyamoto

Takasu

et al. 2020

Toxins

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Cry toxins are insecticidal proteins produced by Bacillus thuringiensis (Bt). They are used commercially to control insect pests since they are very active in specific insects and are harmless to the environment and human health. The gene encoding ATP-binding cassette subfamily A member 2 (ABCA2) was identified in an analysis of Cry2A toxin resistance genes. However, we do not have direct evidence for the role of ABCA2 for Cry2A toxins or why Cry2A toxin resistance does not cross to other Cry toxins. Therefore, we performed two experiments. First, we edited the ABCA2 sequence in Bombyx mori using transcription activator-like effector-nucleases (TALENs) and confirmed the susceptibility-determining ability in a diet overlay bioassay. Strains with C-terminal half-deleted BmABCA2 showed strong and specific resistance to Cry2A toxins; even strains carrying a deletion of 1 to 3 amino acids showed resistance. However, the C-terminal half-deleted strains did not show cross-resistance to other toxins. Second, we conducted a cell swelling assay and confirmed the specific ability of BmABCA2 to Cry2A toxins in HEK239T cells. Those demonstrated that BmABCA2 is a functional receptor for Cry2A toxins and that BmABCA2 deficiency-dependent Cry2A resistance does not confer cross-resistance to Cry1A, Cry1Ca, Cry1Da, Cry1Fa or Cry9Aa toxins.

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“…Overexpression ALP and APN in the insect cells could significantly increase the toxicity of Cry1Ac (Wei, Liang et al, 2016; Wei, Yang et al 2018). Stevens, Song, Bruning, Choo, and Baxter (2017) reported they expressed P. xylostella ABCC2 gene in transgenic Drosophila caused this transgenic Drosophila susceptible to Cry1Ac. Meanwhile, RNA interference (RNAi) and CRISPR/Cas9 technology recently were used to reduce the expression of target genes or proteins to confirm the function of the Cry toxins candidate receptor proteins.…”

Section: Discussionmentioning

confidence: 99%

Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hübner)

Wang

Wei

Wang

et al. 2020

Arch Insect Biochem Physiol

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Polycalin has been confirmed as a binding protein of the Cry toxins in a few Lepidoptera insects, but its function in the action mechanism of Cry1Ac and whether it is involved in resistance evolution are still unclear. In this study, Ligand blot and enzyme‐linked immunosorbent assays showed that Helicoverpa armigera polycalin could specifically interact with Cry1Ac with a high affinity (Kd = 118.80 nM). Importantly, antisera blocking polycalin in H. armigera larvae decreased the toxicity of Cry1Ac by 31.84%. Furthermore, the relative gene and protein expressions were lower in Cry1Ac‐resistant strain (LF60) than that in Cry1Ac‐susceptible strain (LF). These findings indicated that H. armigera polycalin was a possible receptor of Cry1Ac and may be contributed to the resistance to Cry1Ac.

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Expressing a moth abcc2 gene in transgenic Drosophila causes susceptibility to Bt Cry1Ac without requiring a cadherin-like protein receptor

Cited by 49 publications

References 49 publications

Differential side-effects of Bacillus thuringiensis bioinsecticide on non-target Drosophila flies

Differential side-effects of Bacillus thuringiensis bioinsecticide on non-target Drosophila flies

ATP-Binding Cassette Subfamily a Member 2 Is a Functional Receptor for Bacillus thuringiensis Cry2A Toxins in Bombyx mori, But Not for Cry1A, Cry1C, Cry1D, Cry1F, or Cry9A Toxins

Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hübner)

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