Search results for "Cry1A"

showing 10 items of 53 documents

A single type of cadherin is involved inBacillus thuringiensistoxicity inPlutella xylostella

2015

Cadherins have been described as one the main functional receptors for the toxins of the entomopathogenic bacterium, Bacillus thuringiensis (Bt). With the availability of the whole genome of Plutella xylostella, different types of cadherins have been annotated. In this study we focused on determining those members of the cadherin-related proteins that potentially play a role in the mode of action of Bt toxins. For this, we mined the genome of P. xylostella to identify these putative cadherins. The genome screening revealed 52 genes that were annotated as cadherin or cadherin-like genes. Further analysis revealed that six of these putative cadherins had three motifs common to all Bt-related …

GeneticsSignal peptideCadherinfungiRNABiologybiology.organism_classificationMolecular biologyGenomeCry1AcRNA interferenceInsect ScienceBacillus thuringiensisGeneticsMolecular BiologyGeneInsect Molecular Biology
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Mode of inheritance and stability of resistance toBacillus thuringiensis varkurstaki in a diamondback moth (Plutella xylostella) population from Mala…

2000

Genetic inheritance of resistance to Bacillus thuringiensis var kurstaki (BTK) was examined in a diamondback moth (Plutella xylostella) population collected from the Melaka region of Malaysia. A BTK-selected sub-population (BTK-SEL) which was more than 100-fold resistant to BTK compared with a susceptible (ROTH) population of P xylostella was used with standard reciprocal crosses and back-crosses between ROTH and BTK-SEL. Logit regression analysis of F 1 reciprocal crosses indicated that BTK resistance was inherited as an incompletely recessive autosomal trait and controlled by a single locus. In contrast, other studies have shown that resistance to Cry1Ac is inherited as an incompletely do…

Geneticseducation.field_of_studyDiamondback mothPesticide resistancebiologyfungiPopulationPlutellaLocus (genetics)General Medicinebiology.organism_classificationCry1Acimmune system diseaseshemic and lymphatic diseasesInsect ScienceBacillus thuringiensisBotanyAlleleeducationAgronomy and Crop SciencePest Management Science
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Reduced membrane-bound alkaline phosphatase does not affect binding of Vip3Aa in a Heliothis virescens resistant colony

2020

The Vip3Aa insecticidal protein from Bacillus thuringiensis (Bt) is produced by specific transgenic corn and cotton varieties for efficient control of target lepidopteran pests. The main threat to this technology is the evolution of resistance in targeted insect pests and understanding the mechanistic basis of resistance is crucial to deploy the most appropriate strategies for resistance management. In this work, we tested whether alteration of membrane receptors in the insect midgut might explain the &gt

HELIOTHIS-VIRESCENSInsecticidesHealth Toxicology and Mutagenesislcsh:MedicinePROTEIN0601 Biochemistry and Cell BiologyToxicologyBiotecnologiaInsecticide ResistanceBacillus thuringiensisSITES0303 health sciencesbiologyChemistryfood and beveragesPlants Genetically ModifiedLepidopteraBiochemistryFood Science & TechnologyInsect ProteinsAlkaline phosphatase1115 Pharmacology and Pharmaceutical Sciencestobacco budwormLife Sciences & BiomedicineSPODOPTERA-FRUGIPERDA MIDGUTProtein BindingEXPRESSIONBrush borderBacillus thuringiensisCRY1ACArticleVESICLES03 medical and health sciencesBACILLUS-THURINGIENSISBacterial ProteinsDownregulation and upregulationinsecticidal proteinsCell surface receptor<i>Bacillus thuringiensis</i>AnimalsCROPS030304 developmental biologyScience & TechnologyGenetically modified maizeHeliothis virescens030306 microbiologylcsh:RfungiMembrane ProteinsMidgutAlkaline Phosphatasebiology.organism_classificationTOXIN RESISTANCEinsect resistanceProteïnes
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Binding analyses of Cry1Ab and Cry1Ac with membrane vesicles from Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis.

2004

The binding properties of Bacillus thuringiensis toxins to brush border membrane vesicles of Dipel-resistant and -susceptible Ostrinia nubilalis larvae were compared using ligand-toxin immunoblot analysis, surface plasmon resonance (SPR), and radiolabeled toxin binding assays. In ligand-toxin immunoblot analysis, the number of Cry1Ab or Cry1Ac toxin binding proteins and the relative toxin binding intensity were similar in vesicles from resistant and susceptible larvae. Surface plasmon resonance with immobilized activated Cry1Ab toxin indicated that there were no significant differences in binding with fluid-phase vesicles from resistant and susceptible larvae. Homologous competition assays …

InsectaTime FactorsBrush borderBacterial ToxinsImmunoblottingBiophysicsBacillus thuringiensisReceptors Cell SurfacePlasma protein bindingBiologyMothsmedicine.disease_causeLigandsBiochemistryBinding CompetitiveCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding sitePest Control BiologicalMolecular BiologyBinding SitesBacillus thuringiensis ToxinsDose-Response Relationship DrugMicrovilliToxinVesiclefungiCell Membranefood and beveragesCell BiologySurface Plasmon Resonancebiology.organism_classificationMolecular biologyEndotoxinsKineticsmedicine.anatomical_structureCry1AcBiochemistryInsect ProteinsProtein BindingBiochemical and biophysical research communications
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Lack of Detrimental Effects of Bacillus thuringiensis Cry Toxins on the Insect Predator Chrysoperla carnea : a Toxicological, Histopathological, and …

2006

ABSTRACT The effect of Cry proteins of Bacillus thuringiensis on the green lacewing ( Chrysoperla carnea ) was studied by using a holistic approach which consisted of independent, complementary experimental strategies. Tritrophic experiments were performed, in which lacewing larvae were fed Helicoverpa armigera larvae reared on Cry1Ac, Cry1Ab, or Cry2Ab toxins. In complementary experiments, a predetermined amount of purified Cry1Ac was directly fed to lacewing larvae. In both experiments no effects on prey utilization or fitness parameters were found. Since binding to the midgut is an indispensable step for toxicity of Cry proteins to known target insects, we hypothesized that specific bind…

InsectanoctuidaeBacterial ToxinsBacillus thuringiensisHelicoverpa armigeraApplied Microbiology and BiotechnologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyExiguaInvertebrate MicrobiologyAnimalsBioassaycrystal proteinsPest Control BiologicalChrysoperla carnealarval midgutBacillus thuringiensis ToxinsMicrovilliEcologybiologybinding-sitesfungitoxicityMidgutbiology.organism_classificationspodoptera-exiguaEndotoxinsPRI BioscienceBiochemistryCry1Acmaize expressing cry1abNoctuidaeDigestive Systemborder membrane-vesicleshelicoverpa-armigera lepidopteraFood ScienceBiotechnologyresistant transgenic plants
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Screening for Bacillus thuringiensis Crystal Proteins Active against the Cabbage Looper, Trichoplusia ni

2000

Abstract Toxicity tests were performed to find among Cry1 and Cry2 Bacillus thuringiensis crystal proteins those with high activity against the cabbage looper. Tests were performed with neonate larvae on surface-contaminated artificial diet. The crystal proteins found to be toxic were, from higher to lower toxicity: Cry1Ac, Cry1Ab, Cry1C, Cry2Aa, Cry1J, and Cry1F (LC50 of 1.1–4.1, 3.4–4.4, 12, 34, 87, and 250 ng/cm2, respectively). Cry1B, Cry1D, and Cry1E can be considered nontoxic (LC50 higher than 2500 ng/cm2). Cry1Aa was moderately toxic to nontoxic, depending on the source (LC50 of 420 ng/cm2 from PGS and 8100 ng/cm2 from Ecogen). In vitro binding assays with trypsin-activated 125I-labe…

InsecticidesBacillus thuringiensis ToxinsBrush borderBacterial ToxinsfungiBacillus thuringiensisMidgutMothsBiologybiology.organism_classificationBacillalesEndotoxinsIodine RadioisotopesHemolysin ProteinsBacterial ProteinsCry1AcBiochemistryCabbage looperBacillus thuringiensisBotanyToxicityTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsJournal of Invertebrate Pathology
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Synergism and Antagonism between Bacillus thuringiensis Vip3A and Cry1 Proteins in Heliothis virescens, Diatraea saccharalis and Spodoptera frugiperda

2014

Made available in DSpace on 2015-03-18T15:56:04Z (GMT). No. of bitstreams: 0 Previous issue date: 2014-10-02Bitstream added on 2015-03-18T16:28:28Z : No. of bitstreams: 1 WOS000342591500006.pdf: 270331 bytes, checksum: c280e3f5bc5e3bb0b92bf74d046135f0 (MD5) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Spanish Ministry of Economy and Competivity FEDER Second generation Bt crops (insect resistant crops carrying Bacillus thuringiensis genes) combine more than one gene that codes for insecticidal proteins in the same plant to provide better control of agricultural pests. Some of the new combinations involve co-expression of cry and vip genes. Because Cry and Vip proteins …

InsecticidesBacillus thuringiensislcsh:MedicineSpodopteraSpodopteraDiatraea saccharalisHemolysin ProteinsLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyGeneticsEscherichia coliAnimalslcsh:ScienceMolecular BiologyMultidisciplinarybiologyHeliothis virescensBacillus thuringiensis Toxinslcsh:RfungiBiology and Life SciencesAgriculturebiology.organism_classificationEndotoxinsLepidopteraBiochemistryCry1AcLarvalcsh:QElectrophoresis Polyacrylamide GelPest ControlAntagonismZoologyEntomologyResearch ArticleBiotechnologyProtein BindingPLoS ONE
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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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