ATP-binding cassette transporter subfamily C members 2, 3 and cadherin protein are susceptibility-determining factors in Bombyx mori for multiple Bacillus thuringiensis Cry1 toxins

Wang, Yonghao; Adegawa, Satomi; Miyamoto, Kazuhisa; Takasu, Yoko; Iizuka, Tetsuya; Wada, Shinpei; Mang, Dingze; Li, Xiaohua; Kim, Seungwon; Satō, Ryōichi; Watanabe, Kenji

doi:10.1016/j.ibmb.2021.103649

Cited by 9 publications

(43 citation statements)

References 43 publications

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“…The data obtained in the present study confirmed the key role of FAW ABCC2 and ABCC3 as Cry1Ab receptors, but did not suggest functional redundancy of ABCC2 and ABCC3 as Cry1F receptors, as for example shown for Cry1F in B. mori [51], or for Cry1A toxins in H. armigera [52]. We observed no membrane permeabilization in Sf9 cells expressing ABCC3 when incubated with Cry1F, whereas Cry1Ab and Cry1A.105 interacted with both ABCC2 and ABCC3 at low nanomolar concentrations.…”

Section: Discussionsupporting

confidence: 82%

“…There is an emerging body of evidence that ABC-transporters are critical determinants of three-domain (3D) Cry toxin-mediated toxicity and resistance in several lepidopteran species [29,32,33,[49][50][51]. This is also supported by results obtained with ABCC2 knockout lines of S. frugiperda expressing high levels of resistance against Cry1F and Cry1Ab [41].…”

Section: Discussionmentioning

confidence: 93%

“…Studies with genome-edited S. exigua confirmed a crucial role for ABCC2, but not ABCC3 in Cry1F and Cry1Ac toxicity [50]. In B. mori only the double knockout of ABCC2 and ABCC3 conferred Cry1F resistance [51], however, in contrast, the double knockout in FAW was lethal [49].…”

Section: Discussionmentioning

confidence: 99%

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Recombinant Expression of ABCC2 Variants Confirms the Importance of Mutations in Extracellular Loop 4 for Cry1F Resistance in Fall Armyworm

Franz

Raming

Nauen

2022

Toxins

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Fall armyworm (FAW), Spodoptera frugiperda, is a highly destructive and invasive global noctuid pest. Its control is based on insecticide applications and Bacillus thuringiensis (Bt) insecticidal Cry toxins expressed in transgenic crops, such as Cry1F in Bt corn. Continuous selection pressure has resulted in populations that are resistant to Bt corn, particularly in Brazil. FAW resistance to Cry1F was recently shown to be conferred by mutations of ATP-binding cassette transporter C2 (ABCC2), but several mutations, particularly indels in extracellular loop 4 (ECL4), are not yet functionally validated. We addressed this knowledge gap by baculovirus-free insect cell expression of ABCC2 variants (and ABCC3) by electroporation technology and tested their response to Cry1F, Cry1A.105 and Cry1Ab. We employed a SYTOXTM orange cell viability test measuring ABCC2-mediated Bt toxin pore formation. In total, we tested seven different FAW ABCC2 variants mutated in ECL4, two mutants modified in nucleotide binding domain (NBD) 2, including a deletion mutant lacking NBD2, and S. frugiperda ABCC3. All tested ECL4 mutations conferred high resistance to Cry1F, but much less to Cry1A.105 and Cry1Ab, whereas mutations in NBD2 hardly affected Bt toxin activity. Our study confirms the importance of indels in ECL4 for Cry1F resistance in S. frugiperda ABCC2.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 93%

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Recombinant Expression of ABCC2 Variants Confirms the Importance of Mutations in Extracellular Loop 4 for Cry1F Resistance in Fall Armyworm

Franz

Raming

Nauen

2022

Toxins

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“…Liu et al and Zhao et al reported that single knockouts of either PxABCC2 and PxABCC3 caused no or several-fold Cry1Ac resistance but the double knockout of them caused >8000-fold resistance [40,41], suggesting that PxABCC2 and PxABCC3 make the almost same contributions in Cry1Ac susceptibility (Figure 5). Functional redundancy of the two ABC transporters in Cry1Ac and Cry1F susceptibility were reported in other lepidopteran species [39,42]. Thus, the results from Liu et showed >34,000-fold Cry1Ac resistance [72], suggesting that the quadruple knockout disrupts further other synergism(s) requiring other molecule(s) than PxABCC2, PxABCC3, PxAPN1, and PxAPN3a, as the four molecules are suggested to participate in the primary susceptibility determinant.…”

Section: Role Of Apns In Plutellamentioning

confidence: 81%

“…Toxicities predicted using this formula are strongly correlated with the actual synergism-mediated toxicity observed in in vitro assays (R 2 = 0.9039, p < 0.001) (Figure 11), indicating that the Cry-receptor binding affinity explains the synergism-mediated toxicity. [18,34,38,42,89]. Predicted toxicity only indicates an index of the toxicity level and does not predict the actual cell susceptibility threshold of Cry concentration (the unit of predicted toxicity is not M but M 2 ).…”

Section: Explanation and Prediction Of Synergism-mediated Cry Toxicit...mentioning

confidence: 99%

Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin

Endo

2022

Toxins

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Cry proteins from Bacillus thuringiensis (Bt) and other bacteria are pesticidal pore-forming toxins. Since 2010, when the ABC transporter C2 (ABCC2) was identified as a Cry1Ac protein resistant gene, our understanding of the mode of action of Cry protein has progressed substantially. ABCC2 mediates high Cry1A toxicity because of its high activity for helping pore formation. With the discovery of ABCC2, the classical killing model based on pore formation and osmotic lysis became nearly conclusive. Nevertheless, we are still far from a complete understanding of how Cry proteins form pores in the cell membrane through interactions with their host gut membrane proteins, known as receptors. Why does ABCC2 mediate pore formation with high efficiency unlike other Cry1A-binding proteins? Is the “prepore” formation indispensable for pore formation? What is the mechanism underlying the synergism between ABCC2 and the 12-cadherin domain protein? We examine potential mechanisms of pore formation via receptor interactions in this paper by merging findings from prior studies on the Cry mode of action before and after the discovery of ABC transporters as Cry protein receptors. We also attempt to explain Cry toxicity using Cry–receptor binding affinities, which successfully predicts actual Cry toxicity toward cultured cells coexpressing ABC transporters and cadherin.

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Use of gut binding peptides as artificial anchors for bacterial pesticidal proteins

Tavares,

Mishra,

Bonning

2023

Advances in Insect Physiology

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ATP-binding cassette transporter subfamily C members 2, 3 and cadherin protein are susceptibility-determining factors in Bombyx mori for multiple Bacillus thuringiensis Cry1 toxins

Cited by 9 publications

References 43 publications

Recombinant Expression of ABCC2 Variants Confirms the Importance of Mutations in Extracellular Loop 4 for Cry1F Resistance in Fall Armyworm

Recombinant Expression of ABCC2 Variants Confirms the Importance of Mutations in Extracellular Loop 4 for Cry1F Resistance in Fall Armyworm

Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin

Use of gut binding peptides as artificial anchors for bacterial pesticidal proteins

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