Search results for "bacillus thuringiensis"

showing 10 items of 211 documents

A Genomic and Proteomic Approach to Identify and Quantify the Expressed

2018

The combined analysis of genomic and proteomic data allowed us to determine which cry and vip genes are present in a Bacillus thuringiensis (Bt) isolate and which ones are being expressed. Nine Bt isolates were selected from Spanish collections of Bt based on their vip1 and vip2 gene content. As a first step, nine isolates were analyzed by PCR to select those Bt isolates that contained genes with the lowest similarity to already described vip1 and vip2 genes (isolates E-SE10.2 and O-V84.2). Two selected isolates were subjected to a combined genomic and proteomic analysis. The results showed that the Bt isolate E-SE10.2 codifies for two new vegetative proteins, Vip2Ac-like_1 and Sip1Aa-like_…

InsecticidesBacterial Proteinsinsect pest controlBacterial ToxinsBacillus thuringiensiscry proteinsGenomicsvip proteinsArticlecrop protectionToxins
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Different mechanisms of resistance to Bacillus thuringiensis toxins in the indianmeal moth.

2001

ABSTRACT Susceptibility to protoxin and toxin forms of Cry1Ab and the binding of 125 I-labeled Cry1Ab and Cry1Ac has been examined in three Plodia interpunctella colonies, one susceptible (688 s ) and two resistant (198 r and Dpl r ) to Bacillus thuringiensis . Toxicological studies showed that the 198 r colony was 11-fold more resistant to Cry1Ab protoxin than to Cry1Ab activated toxin, whereas the Dpl r colony was 4-fold more resistant to protoxin versus toxin. Binding results with 125 I-labeled toxins indicated the occurrence of two different binding sites for Cry1Ab in the susceptible insects, one of them shared with Cry1Ac. Cry1Ab binding was found to be altered in insects from both re…

InsecticidesBacterial ToxinsBacillus thuringiensisMothsmedicine.disease_causeApplied Microbiology and BiotechnologyBinding CompetitiveMicrobiologyToxicologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineInvertebrate MicrobiologyAnimalsBinding siteProtein PrecursorsLarvaBacillaceaeEcologybiologyBacillus thuringiensis ToxinsMicrovilliToxinParasporal bodyfungibiology.organism_classificationBacillalesEndotoxinsCry1AcLarvaFood ScienceBiotechnologyApplied and environmental microbiology
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Susceptibility of Spodoptera exigua to 9 toxins from Bacillus thuringiensis

2007

Nine of the most common lepidopteran active Cry proteins from Bacillus thuringiensis have been tested for activity against Spodoptera exigua. Because of possible intraspecific variability, three laboratory strains (FRA, HOL, and MUR) have been used. Mortality assays were performed with the three strains. LC(50) values for the active toxins were determined to the FRA and the HOL strains, whereas susceptibility of the MUR strain was assessed using only two concentrations. The results showed that Cry1Ca, Cry1Da, and Cry1Fa were the most effective toxins with all strains. Cry1Ab was found effective for the HOL strain, but very little effective against FRA (6.5-fold) and MUR strains. Cry1Aa and …

InsecticidesBacterial ToxinsLongevityBacillus thuringiensisSpodopteraSpodopteramedicine.disease_causeMicrobiologychemistry.chemical_compoundBacterial ProteinsSpecies SpecificityBacillus thuringiensisBotanyExiguamedicineAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsDose-Response Relationship DrugbiologyStrain (chemistry)Toxinfungibiology.organism_classificationBacillalesCry1AcchemistryLarvaGrowth inhibitionJournal of Invertebrate Pathology
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Mechanism of Resistance to Bacillus thuringiensis Toxin Cry1Ac in a Greenhouse Population of the Cabbage Looper, Trichoplusia ni

2007

ABSTRACT The cabbage looper, Trichoplusia ni , is one of only two insect species that have evolved resistance to Bacillus thuringiensis in agricultural situations. The trait of resistance to B. thuringiensis toxin Cry1Ac from a greenhouse-evolved resistant population of T. ni was introgressed into a highly inbred susceptible laboratory strain. The resulting introgression strain, GLEN-Cry1Ac-BCS, and its nearly isogenic susceptible strain were subjected to comparative genetic and biochemical studies to determine the mechanism of resistance. Results showed that midgut proteases, hemolymph melanization activity, and midgut esterase were not altered in the GLEN-Cry1Ac-BCS strain. The pattern of…

InsecticidesBacterial ToxinsPopulationBacillus thuringiensisDrug ResistanceBrassicaInsect ControlApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsCabbage looperBacillus thuringiensisHemolymphBotanyInvertebrate MicrobiologyTrichoplusiaAnimalseducationeducation.field_of_studyBacillus thuringiensis ToxinsEcologybiologyStrain (chemistry)fungifood and beveragesMidgutbiology.organism_classificationEndotoxinsLepidopteraCry1AcFood ScienceBiotechnologyApplied and Environmental Microbiology
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Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera: Yponomeutidae)

2009

The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larv…

InsecticidesBinding SitesBacillus thuringiensis Toxinsbiologymedia_common.quotation_subjectfungiBiological pest controlInsectMothsPrays oleaebiology.organism_classificationEndotoxinsLepidoptera genitaliaHemolysin ProteinsBiopesticideBacterial ProteinsCry1AcLarvaBacillus thuringiensisBotanyAnimalsPEST analysisPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commonJournal of Invertebrate Pathology
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Overproduction of the Bacillus thuringiensis Vip3Aa16 toxin and study of its insecticidal activity against the carob moth Ectomyelois ceratoniae

2015

Abstract The vip3Aa16 gene of Bacillus thuringiensis strain BUPM95 was cloned and expressed in Escherichia coli . Optimization of Vip3A16 protein expression was conducted using Plackett–Burman design and response surface methodology. Accordingly, the optimum Vip3A16 toxin production was 170 μg/ml at 18 h post-induction time and 39 °C post-induction temperature. This corresponds to an improvement of 21 times compared to the starting conditions. The insecticidal activity, evaluated against Ectomyelois ceratoniae , displayed an LC 50 value of 40 ng/cm 2 and the midgut histopathology of Vip3Aa16 fed larvae showed vacuolization of the cytoplasm, brush border membrane destruction, vesicle formati…

InsecticidesEctomyelois ceratoniaebiologyBrush borderToxinBacillus thuringiensisMidgutMothsbiology.organism_classificationmedicine.disease_causeMicrobiologyBacterial ProteinsVacuolizationBacillus thuringiensismedicineAnimalsOverproductionEscherichia coliEcology Evolution Behavior and SystematicsJournal of Invertebrate Pathology
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Encapsulation of the Bacillus thuringiensis secretable toxins Vip3Aa and Cry1Ia in Pseudomonas fluorescens

2013

Vip3A and Cry1I toxins are secreted during the vegetative growth of Bacillus thuringiensis. Vip3A toxins do not share homology to the crystal (Cry) proteins and are active against a different spectrum of lepidopteran species. Cry1I toxins share similarity with the Cry1 protein group but do not accumulate in the parasporal crystal. Since Vip3A and Cry1I toxins are released from the cell, they are excluded from biological formulates based on spores and crystals of B. thuringiensis. As an approach to obtain novel sprayable insecticides containing Vip3 or Cry1I toxins, Vip3Aa and Cry1Ia proteins were expressed in Pseudomonas fluorescens. This bacterium, non-pathogenic to animals or plants, can …

InsecticidesExpression vectorbiologyBacterial pathogenPseudomonas fluorescensHeterologous expression systemSpodopterabiology.organism_classificationmedicine.disease_causeMicrobial controlMicrobiologyInsect ScienceBacillus thuringiensismedicineBioassayHeterologous expressionAgronomy and Crop ScienceEscherichia coliCry proteinsBacteriaVip proteinsBiological Control
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The Rapid Evolution of Resistance to Vip3Aa Insecticidal Protein in Mythimna separata (Walker) Is Not Related to Altered Binding to Midgut Receptors

2021

Laboratory selection for resistance of field populations is a well-known and useful tool to understand the potential of insect populations to evolve resistance to insecticides. It provides us with estimates of the frequency of resistance alleles and allows us to study the mechanisms by which insects developed resistance to shed light on the mode of action and optimize resistance management strategies. Here, a field population of Mythimna separata was subjected to laboratory selection with either Vip3Aa, Cry1Ab, or Cry1F insecticidal proteins from Bacillus thuringiensis. The population rapidly evolved resistance to Vip3Aa reaching, after eight generations, a level of >3061-fold resistance…

InsecticidesHealth Toxicology and Mutagenesismedia_common.quotation_subjectPopulationBacillus thuringiensisInsectMothsToxicologyInsecticide Resistance03 medical and health sciencesMythimna separataHemolysin ProteinsBacterial ProteinsBacillus thuringiensis<i>Bacillus thuringiensis</i>cross resistanceBt toxinsAnimalseducationCross-resistance030304 developmental biologymedia_commonGenetics0303 health sciencesLarvaeducation.field_of_studybiologyResistance (ecology)Bacillus thuringiensis Toxins030306 microbiologyCommunicationfungiRMidgutbiology.organism_classificationEndotoxinsLarvaoriental armywormMedicineProtein BindingToxins
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Susceptibility of Spodoptera frugiperda and S. exigua to Bacillus thuringiensis Vip3Aa insecticidal protein

2011

The Vip3Aa protein is an insecticidal protein secreted by Bacillus thuringiensis during the vegetative stage of growth. The activity of this protein has been tested after different steps/protocols of purification using Spodoptera frugiperda as a control insect. The results showed that the Vip3Aa protoxin was stable and retained full toxicity after being subjected to common biochemical steps used in protein purification. Bioassays with the protoxin in S. frugiperda and S. exigua showed pronounced differences in LC(50) values when mortality was measured at 7 vs. 10d. At 7d most live larvae were arrested in their development. LC(50) values of "functional mortality" (dead larvae plus larvae rem…

InsecticidesLongevityBacillus thuringiensisInsect pest controlInsect proteaseBacterial ProteinSpodopteraSpodopteraMedian lethal doseMicrobiologyLethal Dose 50Vegetative insecticidal proteinBacterial ProteinsSpecies SpecificityBacillus thuringiensisparasitic diseasesExiguaProtein purificationBotanyAnimalsBacillus thuringiensiBioassayPest Control BiologicalInsecticideEcology Evolution Behavior and SystematicsbiologyAnimalfungiMidgutbiology.organism_classificationBioinsecticideHost-Pathogen InteractionMode of actionLarvaHost-Pathogen InteractionsInstarBiological AssayElectrophoresis Polyacrylamide GelDisease SusceptibilityJournal of Invertebrate Pathology
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Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species

2014

Abstract Vip3 proteins have been described to be secreted by Bacillus thuringiensis during the vegetative growth phase and to display a broad insecticidal spectrum against lepidopteran larvae. Vip3Aa protoxin has been reported to be significantly more toxic to Spodoptera frugiperda than to Spodoptera exigua and differences in the midgut processing have been proposed to be responsible. In contrast, we have found that Vip3Ae is essentially equally toxic against these two species. Proteolysis experiments were performed to study the stability of Vip3A proteins to peptidase digestion and to see whether the differences found could explain differences in toxicity against these two Spodoptera speci…

InsecticidesPhysiologyProteolysisBacterial ProteinSpodopteraSpodopteraMicrobiologyVegetative insecticidal proteinBacterial ProteinsSpecies SpecificitySpodoptera exiguaBacillus thuringiensisExiguamedicineAnimalsPest Control BiologicalMidgut peptidaseInsecticideChymotrypsinbiologymedicine.diagnostic_testAnimalMedicine (all)Serine EndopeptidasesfungiSpodoptera frugiperdaMidgutbiology.organism_classificationTrypsinSerine EndopeptidaseSerine peptidaseBiochemistryMode of actionLarvaInsect Sciencebiology.proteinDigestionDigestive Systemmedicine.drugJournal of Insect Physiology
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