Comparative binding of Cry1Ab and Cry1F Bacillus thuringiensis toxins to brush border membrane proteins from Ostrinia nubilalis, Ostrinia furnacalis and Diatraea saccharalis (Lepidoptera: Crambidae) midgut tissue

Tan, Sek Yee; Cayabyab, Bonifacio F.; Alcantara, Edwin P.; Huang, Fangneng; He, Kanglai; Nickerson, Kenneth W.; Siegfried, Blair D.

doi:10.1016/j.jip.2013.08.007

Cited by 17 publications

(12 citation statements)

References 43 publications

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“…Moreover, it has also been described the occurrence of shared binding sites among Cry1A proteins and Cry1Fa for some insect species (Banks et al, 2001;Hernández and Ferré, 2005;Hernández-Rodríguez et al, 2013). Interestingly, an early report on D. saccharalis described that both Cry1Ab and Cry1F proteins bound to a 210 kDa protein using ligand blot analysis (Tan et al, 2013), in agreement with the binding results obtained in this study.…”

Section: Introductionsupporting

confidence: 91%

Binding analysis of Bacillus thuringiensis Cry1 proteins in the sugarcane borer, Diatraea saccharalis (Lepidoptera: Crambidae)

Davolos

Hernández‐Martínez

Crialesi-Legori

et al. 2015

Journal of Invertebrate Pathology

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Section: Introductionsupporting

confidence: 91%

Binding analysis of Bacillus thuringiensis Cry1 proteins in the sugarcane borer, Diatraea saccharalis (Lepidoptera: Crambidae)

Davolos

Hernández‐Martínez

Crialesi-Legori

et al. 2015

Journal of Invertebrate Pathology

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“…There are eight orthologous apn genes, apn 1 thru apn 8, which resulted from ancestral tandem duplication in the lepidopteran lineage 116 - 118 , and confirmed to occur in O. nubilalis by genetic linkage and physical mapping 31 . Of these orthologs, apn 1 and apn 3 are identified as Cry1A toxin receptors in O. nubilalis 44 and O. furnacalis 43 . Experimental evidence also shows that the O. nubilalis apn 1 (On apn 1) gene product expressed in the surface of cultured cells bind Cry1Ab toxins in vivo , and OnAPN3a and OnAPN8 peptides analogously bind Cry1Fa 84 .…”

Section: Discussionmentioning

confidence: 99%

“…A cell adhesion protein, cadherin ( cad ), was identified as an in vitro Cry1A toxin receptor in the midgut of M. sexta 42 , and an ortholog from O. nubilalis analogously is capable of binding Cry1Ab, Cry1Ac and Cry1F toxins in vitro 43 , 44 as well as Cry1A toxins in vivo 45 . A mutation caused by transposon insertion into the H. virescens cad provided the initial evidence for involvement in resistance mechanisms 46 , and additional mutations were associated with Bt resistance traits among field-derived Pectinophora possypiella 12 , H. armigera 47 , and O. furnacalis 48 .…”

Section: Introductionmentioning

confidence: 99%

Down-regulation of aminopeptidase N and ABC transporter subfamily G transcripts in Cry1Ab and Cry1Ac resistant Asian corn borer, Ostrinia furnacalis (Lepidoptera: Crambidae)

Zhang¹,

Coates²,

Wang³

et al. 2017

Int. J. Biol. Sci.

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The Asian corn borer (ACB), Ostrinia furnacalis (Lepidoptera: Crambidae), is a highly destructive pest of cultivated maize throughout East Asia. Bacillus thuringiensis (Bt) crystalline protein (Cry) toxins cause mortality by a mechanism involving pore formation or signal transduction following toxin binding to receptors along the midgut lumen of susceptible insects, but this mechanism and mutations therein that lead to resistance are not fully understood. In the current study, quantitative comparisons were made among midgut expressed transcripts from O. furnacalis susceptible (ACB-BtS) and laboratory selected strains resistant to Cry1Ab (ACB-AbR) and Cry1Ac toxins (ACB-AcR) when feeding on non-Bt diet. From a combined de novo transcriptome assembly of 83,370 transcripts, ORFs of ≥ 100 amino acids were predicted and annotated for 28,940 unique isoforms derived from 12,288 transcripts. Transcriptome-wide expression estimated from RNA-seq read depths predicted significant down-regulation of transcripts for previously known Bt resistance genes, aminopeptidase N1 (apn1) and apn3, as well as a putative ATP binding cassette transporter group G (abcg) gene in both ACB-AbR and -AcR (log2[fold-change] ≥ 1.36; P < 0.0001). The transcripts that were most highly differentially regulated in both ACB-AbR and -AcR compared to ACB-BtS (log2[fold-change] ≥ 2.0; P < 0.0001) included up- and down-regulation of serine proteases, storage proteins and cytochrome P450 monooxygenases, as well as up-regulation of genes with predicted transport function. This study predicted the significant down-regulation of transcripts for previously known Bt resistance genes, aminopeptidase N1 (apn1) and apn3, as well as abccg gene in both ACB-AbR and -AcR. These data are important for the understanding of systemic differences between Bt resistant and susceptible genotypes.

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“…In contrast, the signal transduction model proposes that the binding of the Bt toxin to specific receptors stimulate the G-protein coupled signaling pathway leading to activation of protein kinase A and apoptosis [ 10 ]. The specific cell receptors that Cry1F toxins interact with and lead to subsequent toxicity have yet to be identified for O. nubilalis [ 11 ], although cadherin and aminopeptidases have been implicated based on ligand blot assays [ 12 , 13 ]. Furthermore, Cry1Ab and Cry1Fa were shown to compete for one or more of the same O. nubilalis midgut receptors [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

Transcriptional analysis of susceptible and resistant European corn borer strains and their response to Cry1F protoxin

et al. 2015

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BackgroundDespite a number of recent reports of insect resistance to transgenic crops expressing insecticidal toxins from Bacillus thuringiensis (Bt), little is known about the mechanism of resistance to these toxins. The purpose of this study is to identify genes associated with the mechanism of Cry1F toxin resistance in European corn borer (Ostrinia nubilalis Hübner). For this, we compared the global transcriptomic response of laboratory selected resistant and susceptible O. nubilalis strain to Cry1F toxin. We further identified constitutive transcriptional differences between the two strains.ResultsAn O. nubilalis midgut transcriptome of 36,125 transcripts was assembled de novo from 106 million Illumina HiSeq and Roche 454 reads and used as a reference for estimation of differential gene expression analysis. Evaluation of gene expression profiles of midgut tissues from the Cry1F susceptible and resistant strains after toxin exposure identified a suite of genes that responded to the toxin in the susceptible strain (n = 1,654), but almost 20-fold fewer in the resistant strain (n = 84). A total of 5,455 midgut transcripts showed significant constitutive expression differences between Cry1F susceptible and resistant strains. Transcripts coding for previously identified Cry toxin receptors, cadherin and alkaline phosphatase and proteases were also differentially expressed in the midgut of the susceptible and resistant strains.ConclusionsOur current study provides a valuable resource for further molecular characterization of Bt resistance and insect response to Cry1F toxin in O. nubilalis and other pest species.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-015-1751-6) contains supplementary material, which is available to authorized users.

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Comparative binding of Cry1Ab and Cry1F Bacillus thuringiensis toxins to brush border membrane proteins from Ostrinia nubilalis, Ostrinia furnacalis and Diatraea saccharalis (Lepidoptera: Crambidae) midgut tissue

Cited by 17 publications

References 43 publications

Binding analysis of Bacillus thuringiensis Cry1 proteins in the sugarcane borer, Diatraea saccharalis (Lepidoptera: Crambidae)

Binding analysis of Bacillus thuringiensis Cry1 proteins in the sugarcane borer, Diatraea saccharalis (Lepidoptera: Crambidae)

Down-regulation of aminopeptidase N and ABC transporter subfamily G transcripts in Cry1Ab and Cry1Ac resistant Asian corn borer, Ostrinia furnacalis (Lepidoptera: Crambidae)

Transcriptional analysis of susceptible and resistant European corn borer strains and their response to Cry1F protoxin

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