Search results for "ostrinia"

showing 10 items of 22 documents

Quantitative genetic analysis of Cry1Ab tolerance in Ostrinia nubilalis Spanish populations

2013

30 p.-2 fig.-3 tab.

European corn borerInsecticidesOffspringEuropean corn borerBacillus thuringiensisMothsGenetic analysisOstriniaLepidoptera genitaliaInsecticide ResistanceHeritabilityHemolysin ProteinsBacterial ProteinsBacillus thuringiensisToxicity TestsAnimalsGeneEcology Evolution Behavior and SystematicsGeneticsbiologyBacillus thuringiensis ToxinsfungiPartial resistance allelesfood and beveragesHeritabilitybiology.organism_classificationCadherinsEPIC-PCREndotoxinsSpainCadherinInsect Proteins
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Midgut aminopeptidase N isoforms from Ostrinia nubilalis: Activity characterization and differential binding to Cry1Ab and Cry1Fa proteins from Bacil…

2013

Aminopeptidase N (APN) isoforms from Lepidoptera are known for their involvement in the mode of action of insecticidal Cry proteins from Bacillus thuringiensis. These enzymes belong to a protein family with at least eight different members that are expressed simultaneously in the midgut of lepidopteran larvae. Here, we focus on the characterization of the APNs from Ostrinia nubilalis (OnAPNs) to identify potential Cry receptors. We expressed OnAPNs in insect cells using a baculovirus system and analyzed their enzymatic activity by probing substrate specificity and inhibitor susceptibility. The interaction with Cry1Ab and Cry1Fa proteins (both found in transgenic insect-resistant maize) was …

Gene isoformendocrine systemCD13 AntigensMothsBiochemistrySubstrate SpecificityOstriniaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisToxicity TestsSf9 CellsAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis ToxinsbiologyfungiMidgutbiology.organism_classificationLigand (biochemistry)Molecular biologyEndotoxinsGastrointestinal TractIsoenzymesBlotEnzymechemistryBiochemistryInsect ScienceProtein BindingInsect Biochemistry and Molecular Biology
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Different binding sites for Bacillus thuringiensis Cry1Ba and Cry9Ca proteins in the European corn borer, Ostrinia nubilalis (Hübner).

2014

Binding studies using (125)I-Cry9Ca and biotinylated-Cry1Ba proteins showed the occurrence of independent binding sites for these proteins in Ostrinia nubilalis. Our results, along with previously available binding data, indicate that combinations of Cry1A or Cry1Fa proteins with Cry1Ba and/or Cry9Ca could be a good strategy for the resistance management of O. nubilalis.

GeneticsEuropean corn borerBinding SitesbiologyBacillus thuringiensis ToxinsfungiMothsbiology.organism_classificationZea maysOstriniaEndotoxinsInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisAnimalsBinding sitePest Control BiologicalEcology Evolution Behavior and SystematicsJournal of invertebrate pathology
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Domain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pests

2020

The bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested…

InsecticidesAsiaInsectaHealth Toxicology and Mutagenesismedicine.medical_treatmentBacillus thuringiensislcsh:MedicineSpodopteraToxicologyArticleLethal Dose 5003 medical and health sciencesHelicoverpa armigeraBacterial ProteinsProtein DomainsBacillus thuringiensismedicineAnimalsSpodoptera littoralisPest Control Biological030304 developmental biologychemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyProtein Stabilitylcsh:RfungiSpodoptera spp.Ostrinia furnacalisSouth Americabiology.organism_classificationFusion proteinAnticarsia gemmatalisAmino acidEuropeAnticarsia gemmatalisspodoptera spp. helicoverpa armigeraBiochemistrychemistryAfricaNorth AmericaMamestra brassicaeOstrinia furnacalis
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Study of the bacillus thuringiensis Cry1Ia protein oligomerization promoted by midgut brush border membrane vesicles of lepidopteran and coleopteran …

2020

Bacillus thuringiensis (Bt) produces insecticidal proteins that are either secreted during the vegetative growth phase or accumulated in the crystal inclusions (Cry proteins) in the stationary phase. Cry1I proteins share the three domain (3D) structure typical of crystal proteins but are secreted to the media early in the stationary growth phase. In the generally accepted mode of action of 3D Cry proteins (sequential binding model), the formation of an oligomer (tetramer) has been described as a major step, necessary for pore formation and subsequent toxicity. To know if this could be extended to Cry1I proteins, the formation of Cry1Ia oligomers was studied by Western blot, after the incuba…

Leptinotarsa decemlineataBrush borderHealth Toxicology and MutagenesisBacillus thuringiensislcsh:MedicineSf21 cell lineOstrinia nubilalisToxicologyOligomer formationHemolysin Proteins<i>leptinotarsa decemlineata</i>03 medical and health sciencesWestern blotBacillus thuringiensisLobesia botranaSf9 CellsmedicineAnimalsProtein oligomerizationCry1AbIncubation<i>ostrinia nubilalis</i>030304 developmental biology0303 health sciencesBinding SitesBacillus thuringiensis ToxinsMicrovillimedicine.diagnostic_testbiology030306 microbiologyChemistryCommunicationVesiclelcsh:RfungiMembrane ProteinsMidgut<i>lobesia botrana</i>Trypsinbiology.organism_classificationColeopteraEndotoxinsLepidopteraBiochemistryBioassayProtein MultimerizationProtein Bindingmedicine.drug
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Variability in the cadherin gene in an Ostrinia nubilalis strain selected for Cry1Ab resistance

2008

Transgenic corn expressing Cry1Ab (a Bacillus thuringiensis toxin) is highly effective in the control of Ostrinia nubilalis. For its toxic action, Cry1Ab has to bind to specific insect midgut proteins. To date, in three Lepidoptera species resistance to a Cry1A toxin has been conferred by mutations in cadherin, a protein of the Lepidoptera midgut membrane. The implication of cadherin in the resistance of an Ostrinia nubilalis colony (Europe-R) selected with Bacillus thuringiensis Cry1Ab protoxin was investigated. Several major mutations in the cadherin (cdh) gene were found, which introduced premature termination codons and/or large deletions (ranging from 1383 to 1701bp). The contribution …

MutantDrug ResistanceGenetically modified cropsMothsBiologyBiochemistryOstriniaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyGenetic variationAnimalsMolecular BiologyGeneGeneticsPolymorphism GeneticBacillus thuringiensis ToxinsCadherinfungiGenetic Variationfood and beveragesMidgutCadherinsbiology.organism_classificationEndotoxinsInsect ScienceMutationInsect ProteinsInsect Biochemistry and Molecular Biology
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Susceptibility of ostrinia nubilalis to bacillus thuringiensis var. kurstaki

2003

Baseline susceptibility of European corn borer larvae, Ostrinia nubilalis (Hübner), to a commercial formulation of Bacillus thuringiensis var. kurstaki was determined for different strains in 7 geographic locations in the corn area of North Italy (Po Valley). For the bioassay 7 different doses, raised on a meredic diet, were used and the data was analysed with the Probit analysis. Differences in the susceptibility among the northern Italian populations of O. nubilalis were recorded, which can be attributed to natural variability. The ECB collected near Como and Torino was the most susceptible, respectively with LC50 of 0.23 and 0.57 mg/ml. The most tolerant ones were the larvae coming from …

Settore AGR/11 - Entomologia Generale E ApplicataBacillus thuringiensis Bt European corn borer insecticide resistance Ostrinia nubilalis
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Study of the aminopeptidase N gene family in the lepidopterans Ostrinia nubilalis (Hübner) and Bombyx mori (L.): Sequences, mapping and expression

2010

Aminopeptidases N (APNs) are a class of ectoenzymes present in lepidopteran larvae midguts, involved in the Bacillus thuringiensis (Bt) toxins mode of action. In the present work, seven aminopeptidases have been cloned from the midgut of Ostrinia nubilalis, the major Lepidopteran corn pest in the temperate climates. Six sequences were identified as APNs because of the presence of the HEXXH(X)18E and GAMEN motifs, as well as the signal peptide and the GPI-anchor sequences. The remaining sequence did not contain the two cellular targeting signals, indicating it belonged to the puromycin-sensitive aminopeptidase (PSA) family. An in silico analysis allowed us to find orthologous sequences in Bo…

animal structuresGenetic LinkageSequence analysisMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentBt toxin-binding proteinCD13 AntigensMothsBiochemistryAminopeptidaseOstriniaPuromycin-Sensitive AminopeptidaseQuantitative PCRMidgut APNSequence Analysis ProteinBombyx moriSequence Homology Nucleic AcidBacillus thuringiensisAnimalsAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyGenePhylogenyGeneticsbiologyLarval development expressionGene Expression ProfilingfungiComputational BiologyBombyxbiology.organism_classificationMolecular biologyIsoenzymesSettore BIO/18 - GeneticaSettore AGR/11 - Entomologia Generale E ApplicataLarvaMultigene FamilyInsect ScienceInsect ProteinsPuromycin-sensitive aminopeptidaseSequence Alignment
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A screening of five Bacillus thuringiensis Vip3A proteins for their activity against lepidopteran pests

2014

Five Bacillus thuringiensis Vip3A proteins (Vip3Aa, Vip3Ab, Vip3Ad, Vip3Ae and Vip3Af) and their corresponding trypsin-activated toxins were tested for their toxicity against eight lepidopteran pests: Agrotis ipsilon, Helicoverpa armigera, Mamestra brassicae, Spodoptera exigua, Spodoptera frugiperda, Spodoptera littoralis, Ostrinia nubilalis and Lobesia botrana. Toxicity was first tested at a high dose at 7 and 10. days. No major differences were found when comparing protoxins vs. trypsin-activated toxins. The proteins that were active against most of the insect species were Vip3Aa, Vip3Ae and Vip3Af, followed by Vip3Ab. Vip3Ad was non-toxic to any of the species tested. Considering the res…

biologyfungiMolecular Sequence DataAgrotis ipsilonSpodopteraHelicoverpa armigerabiology.organism_classificationLobesia botranaPlants Genetically ModifiedOstriniaMicrobiologyInsecticide ResistanceLepidopteraBacterial ProteinsBacillus thuringiensisBotanyExiguaAnimalsAmino Acid SequenceSpodoptera littoralisPest Control BiologicalEcology Evolution Behavior and Systematics
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Susceptibility to Cry proteins of a SpanishOstrinia nubilalisglasshouse population repeatedly sprayed withBacillus thuringiensisformulations

2013

Ostrinia nubilalis Hubner (Lepidoptera: Crambidae), a major pest of corn in temperate climates, can feed on other crops due to its polyphagous behaviour. In particular, this species became a serious problem in some sweet pepper commercial glasshouses in south-eastern Spain repeatedly sprayed with Bacillus thuringiensis (Bt) products to control Spodoptera exigua Hubner (Lepidoptera: Noctuidae). The susceptibility of an O. nubilalis colony established from individuals collected in these Bt-sprayed glasshouses was compared with a reference laboratory colony. Differences in susceptibility between the two colonies to Cry1Aa, Cry1Ab, Cry1Ac and Cry2Aa proteins were found. However, our results ind…

education.field_of_studyEuropean corn borerbiologyfungiPopulationfood and beveragesbiology.organism_classificationOstriniaLepidoptera genitaliaHorticultureCry1AcCrambidaeAgronomyInsect ScienceBacillus thuringiensisNoctuidaeeducationAgronomy and Crop ScienceJournal of Applied Entomology
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