IDENTIFICATION OF A CALMODULIN‐BINDING SITE WITHIN THE DOMAIN <scp>I</scp> OF <i><scp>B</scp>ACILLUS THURINGIENSIS</i><scp>C</scp>ry3<scp>A</scp>a TOXIN

Ochoa-Campuzano, Camila; Sánchez, Jorge; García-Robles, Inmaculada; Rausell, Carolina

doi:10.1002/arch.21044

Cited by 3 publications

(3 citation statements)

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“…On L. decemlineata , it has been shown that ADAM metalloprotease serves as receptor for Cry3Aa toxin [68]. Cry3Aa toxin specifically binds to calmodulin (CalM) in a calcium-independent manner [69] and also to the toxin-binding fragments of cadherin [70]. We have taken in consideration these three genes in our analyses and using scientific literature, we built a catalog of those genes known to be involved in resistance to Bt, including several transcripts recently isolated from Diabrotica virgifera showing responses to the Bt toxin Cry3Bb1 [71].…”

Section: Resultsmentioning

confidence: 99%

Sequencing, De Novo Assembly and Annotation of the Colorado Potato Beetle, Leptinotarsa decemlineata, Transcriptome

et al. 2014

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BackgroundThe Colorado potato beetle (Leptinotarsa decemlineata) is a major pest and a serious threat to potato cultivation throughout the northern hemisphere. Despite its high importance for invasion biology, phenology and pest management, little is known about L. decemlineata from a genomic perspective. We subjected European L. decemlineata adult and larval transcriptome samples to 454-FLX massively-parallel DNA sequencing to characterize a basal set of genes from this species. We created a combined assembly of the adult and larval datasets including the publicly available midgut larval Roche 454 reads and provided basic annotation. We were particularly interested in diapause-specific genes and genes involved in pesticide and Bacillus thuringiensis (Bt) resistance.ResultsUsing 454-FLX pyrosequencing, we obtained a total of 898,048 reads which, together with the publicly available 804,056 midgut larval reads, were assembled into 121,912 contigs. We established a repository of genes of interest, with 101 out of the 108 diapause-specific genes described in Drosophila montana; and 621 contigs involved in insecticide resistance, including 221 CYP450, 45 GSTs, 13 catalases, 15 superoxide dismutases, 22 glutathione peroxidases, 194 esterases, 3 ADAM metalloproteases, 10 cadherins and 98 calmodulins. We found 460 putative miRNAs and we predicted a significant number of single nucleotide polymorphisms (29,205) and microsatellite loci (17,284).ConclusionsThis report of the assembly and annotation of the transcriptome of L. decemlineata offers new insights into diapause-associated and insecticide-resistance-associated genes in this species and provides a foundation for comparative studies with other species of insects. The data will also open new avenues for researchers using L. decemlineata as a model species, and for pest management research. Our results provide the basis for performing future gene expression and functional analysis in L. decemlineata and improve our understanding of the biology of this invasive species at the molecular level.

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Section: Resultsmentioning

confidence: 99%

Sequencing, De Novo Assembly and Annotation of the Colorado Potato Beetle, Leptinotarsa decemlineata, Transcriptome

et al. 2014

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“…Previous studies have shown that the ADAM metalloprotease serves as a receptor for the Cry3Aa toxin in L. decemlineata (Ochoa-Campuzano et al 2007). Additionally, the Cry3Aa toxin also binds to calmodulin in a calcium-independent manner (Ochoa-Campuzano et al 2012) and to cadherin fragments (Park et al 2009). By using a pyrosequencing strategy on the 454-FLX platform of Roche, Kumar et al identified 621 contigs involved in insecticide resistance; of these three contigs belonged to metalloprotease ADAM, 10 to cadherin, and 98 to calmodulin, among others (Kumar et al 2014).…”

Section: Transcriptome As Tool To Identify New Proteins Involved In Tmentioning

confidence: 99%

Identification and Characterization of Receptors for Insecticidal Toxins from Bacillus thuringiensis

Grande-Cano¹,

Gómez

2015

Soil Biology

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During the stationary phase of the life cycle of Bacillus thuringiensis (Bt) is produced a parasporal body (crystal) containing insecticidal proteins called Cry toxins, which are used for development of transgenic crops and spray formulations for control of pest insects (Van Rie 2000). Although Bt has been used for two decades as a commercial biopesticide, the mode of action has only been described recently. Cry proteins are included into the pore-forming toxins (PFTs), one of the largest classes of bacterial toxins ). Many sequences of cry genes have been identified, including 56 families (Cry1-Cry56) and 180 subtypes (Cry1Aa, Cry4Ba, etc.). Of all of these proteins, some structures have been resolved by X-ray crystallography. It is interesting to note that the sequences are different but the structural topology is conserved, indicating a similar mechanism of action. All contain three structural domains: Domain I contains seven α-helixes and is involved in the oligomerization of the toxin and its insertion into the membrane, and Domains II and III are made up of β-sheets and are involved in the attachment to the receptors (Soberon et al. 2010).The mechanism of toxicity begins when the insect ingests food contaminated with spores; the crystal is then solubilized in the midgut, releasing protoxins which are activated by proteases, and the toxic fragment binds in sequential fashion to receptors located in the microvilli. The first receptor is a cadherin-like protein (CADP), whose interaction allows the oligomerization of the toxin. This oligomeric

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“…The mode of action of Cry proteins from B. thuringiensis has been extensively studied, especially for lepidopteran-active Cry proteins (Bravo et al., 2007, Vachon et al., 2012; Adang et al., 2014), whereas much less is known for coleopteran-active Cry proteins (Hernández-Martínez et al., 2014, Ochoa-Campuzano et al., 2012, Rausell et al., 2004, Rausell et al., 2007, Slaney et al., 1992). The proposed model starts after the ingestion of the crystals by susceptible insect larvae, followed by crystal solubilization and protease activation in the midgut environment.…”

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confidence: 99%

Unshared binding sites for Bacillus thuringiensis Cry3Aa and Cry3Ca proteins in the weevil Cylas puncticollis (Brentidae)

Hernández‐Martínez

Vera-Velasco

Escriche

2016

Toxicon

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Bacillus thuringiensis Cry3Aa and Cry3Ca proteins have been reported to be toxic against the African sweetpotato pest Cylas puncticollis. In the present work, the binding sites of these proteins in C. puncticollis brush border vesicles suggest the occurrence of different binding sites, but only one of them is shared. Our results suggest that pest resistance mediated by alteration of the shared Cry-receptor binding site might not render both Cry proteins ineffective.

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IDENTIFICATION OF A CALMODULIN‐BINDING SITE WITHIN THE DOMAIN I OF BACILLUS THURINGIENSISCry3Aa TOXIN

Cited by 3 publications

References 29 publications

Sequencing, De Novo Assembly and Annotation of the Colorado Potato Beetle, Leptinotarsa decemlineata, Transcriptome

Sequencing, De Novo Assembly and Annotation of the Colorado Potato Beetle, Leptinotarsa decemlineata, Transcriptome

Identification and Characterization of Receptors for Insecticidal Toxins from Bacillus thuringiensis

Unshared binding sites for Bacillus thuringiensis Cry3Aa and Cry3Ca proteins in the weevil Cylas puncticollis (Brentidae)

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