Search results for "bacillus thuringiensis"

showing 10 items of 211 documents

Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (…

2004

AbstractBinding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis δ-endotoxins.In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry…

ProteasesBrush borderBacterial ToxinsBacillus thuringiensisBiophysicsmedicine.disease_causeBinding CompetitiveBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsProtoxin activationBinding siteProtein PrecursorsChymotrypsinBinding SitesbiologyBacillus thuringiensis ToxinsMicrovilliToxinColorado potato beetleCell MembranefungiCell Biologybiology.organism_classificationTrypsinColeopteraEndotoxinsBiochemistryMode of actionbiology.proteinmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum*

2013

Understanding how Bacillus thuringiensis (Bt) toxins interact with proteins in the midgut of susceptible coleopteran insects is crucial to fully explain the molecular bases of Bt specificity and insecticidal action. In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sodium solute symporter (TcSSS) have been identified by ligand blot as putative Cry3Ba toxin-binding proteins in Tribolium castaneum (Tc) larvae. RNA interference knockdown of TcCad1 or TcSSS proteins resulted in decreased susceptibility to Cry3Ba toxin, demonstrating the Cry toxin receptor functionality for these proteins. In contrast, TcAPN-I silencing had no effect on Cry3Ba larval toxicity, suggesting that th…

ImmunoblottingMolecular Sequence DataReceptors Cell SurfacePlasma protein bindingBiologyCD13 Antigensmedicine.disease_causeBiochemistrySodium-solute symporterdigestive systemMicrobiologyEpitopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisparasitic diseasesmedicineAnimalsAmino Acid SequenceReceptorMolecular BiologyPeptide sequenceTriboliumBinding SitesBacillus thuringiensis ToxinsSequence Homology Amino AcidSymportersCadherinToxinfungiSodiumCell Biologybiology.organism_classificationCadherinsEndotoxinsBiochemistrySymporterbacteriaInsect ProteinsRNA InterferenceProtein Binding
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Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis

2017

Vip3 proteins are secretable proteins from Bacillus thuringiensis whose mode of action is still poorly understood. In this study, the activation process for Vip3 proteins was closely examined in order to better understand the Vip3Aa protein stability and to shed light on its structure. The Vip3Aa protoxin (of 89 kDa) was treated with trypsin at concentrations from 1:100 to 120:100 (trypsin:Vip3A, w:w). If the action of trypsin was not properly neutralized, the results of SDS-PAGE analysis (as well as those with Agrotis ipsilon midgut juice) equivocally indicated that the protoxin could be completely processed. However, when the proteolytic reaction was efficiently stopped, it was revealed t…

0301 basic medicineProteasesHealth Toxicology and MutagenesisSize-exclusion chromatographyBeta sheetBacillus thuringiensislcsh:MedicineBiologyToxicologyCleavage (embryo)ArticleProtein Structure Secondary03 medical and health sciencestrypsin inhibitorsBacterial ProteinsSDS-PAGE artefactprotease stabilitymedicinebacterial secreted proteinsAnimalsTrypsinMode of actionProtein secondary structureVip proteinsIntestinal Secretionslcsh:Rtoxin activationVip proteins; bacterial secreted proteins; toxin activation; proteolytic activation; trypsin inhibitors; <i>Bacillus thuringiensis</i>; SDS-PAGE artefact; protease stabilityTrypsinMolecular biologyLepidoptera030104 developmental biologyBiochemistryproteolytic activationLarvaProteolysisPeptidesAlpha helixmedicine.drugToxins
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A mathematical model of exposure of nontarget Lepidoptera to Bt-maize pollen expressing Cry1Ab within Europe

2010

Genetically modified (GM) maize MON810 expresses a Cry1Ab insecticidal protein, derived from Bacillus thuringiensis ( Bt ), toxic to lepidopteran target pests such as Ostrinia nubilalis . An environmental risk to non-target Lepidoptera from this GM crop is exposure to harmful amounts of Bt -containing pollen deposited on host plants in or near MON810 fields. An 11-parameter mathematical model analysed exposure of larvae of three non-target species: the butterflies Inachis io (L.), Vanessa atalanta (L.) and moth Plutella xylostella (L.), in 11 representative maize cultivation regions in four European countries. A mortality–dose relationship was integrated with a dose–distance relationship t…

1001genetically modified maize Cry1Ab non-target Lepidoptera mathematical model exposure risk assessment60Bacillus thuringiensismedicine.disease_causeZea maysModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyOstriniaExposureCropLepidoptera genitaliaHemolysin ProteinsMathematical modelBacterial ProteinsResearch articlesPollenBacillus thuringiensismedicineAnimalsPest Control BiologicalGeneral Environmental ScienceRisk assessmentGenetically modified maize31General Immunology and MicrobiologybiologyBacillus thuringiensis Toxinsbusiness.industryfungiPest controlPlutellafood and beveragesGeneral MedicineNon-target lepidopterabiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraAgronomyGenetically modified maizePollenCry1abGeneral Agricultural and Biological SciencesbusinessButterflies
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Monitoring of Bacillus Thuringiensis Cry3Aa Toxin Pore Formation using Artificial Bilayer Array with Fused Brush Border Membrane Vesicles from Colora…

2017

LarvaBrush borderbiologyToxinBilayerVesicleBacillus thuringiensisColorado potato beetleBiophysicsmedicinebiology.organism_classificationmedicine.disease_causeMicrobiologyBiophysical Journal
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Toxicity of several d-endotoxins of Bacillus thuringiensis against Helicoverpa armigera (Lepidoptera: Noctuidae) from Spain

2005

Abstract Toxicity and larval growth inhibition of 11 insecticidal proteins of Bacillus thuringiensis were evaluated against neonate larvae of Helicoverpa armigera, a major pest of important crops in Spain and other countries, by a whole-diet contamination method. The most active toxins were Cry1Ac4 and Cry2Aa1, with LC50 values of 3.5 and 6.3 μg/ml, respectively. At the concentrations tested, Cry1Ac4, Cry2Aa1, Cry9Ca, Cry1Fa1, Cry1Ab3, Cry2Ab2, Cry1Da, and Cry1Ja1, produced a significant growth inhibition, whereas Cry1Aa3, Cry1Ca2, and Cry1Ea had no effect.

Veterinary medicineBiological pest controlBacillus thuringiensisHelicoverpa armigeraLepidoptera genitaliachemistry.chemical_compoundHelicoverpa armigeraBacillus thuringiensisBotanyAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsbiologyfungiICPbiology.organism_classificationEndotoxinsLepidopteraBiopesticideMicrobial insect controlchemistrySpainGrowth inhibitionLarvaNoctuidaeCotton pestsCry toxinsPEST analysisGrowth inhibition
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Extent of variation of the Bacillus thuringiensis toxin reservoir: the case of the geranium bronze, Cacyreus marshalli butler (Lepidoptera: Lycaenida…

2002

ABSTRACT Despite the fact that around 200 cry genes from Bacillus thuringiensis have already been cloned, only a few Cry proteins are toxic towards a given pest. A crucial step in the mode of action of Cry proteins is binding to specific sites in the midgut of susceptible insects. Binding studies in insects that have developed cross-resistance discourage the combined use of Cry proteins sharing the same binding site. If resistance management strategies are to be implemented, the arsenal of Cry proteins suitable to control a given pest may be not so vast as it might seem at first. The present study evaluates the potential of B. thuringiensis for the control of a new pest, the geranium bronze…

endocrine systemBacterial ToxinsBacillus thuringiensisZoologymedicine.disease_causeApplied Microbiology and BiotechnologyBinding CompetitiveLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanymedicineInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalBinding SitesEcologybiologyBacillus thuringiensis ToxinsToxinGeranium bronzefungiLycaenidaeMidgutPlantsbiology.organism_classificationEndotoxinsLepidopteraPEST analysisFood ScienceBiotechnologyApplied and environmental microbiology
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Characterization of Bacillus thuringiensis isolates by their insecticidal activity and their production of Cry and Vip3 proteins.

2018

WOS: 000449027600099 PubMed ID: 30383811 Bacillus thuringiensis (Bt) constitutes the active ingredient of many successful bioinsecticides used in agriculture. In the present study, the genetic diversity and toxicity of Bt isolates was investigated by characterization of native isolates originating from soil, fig leaves and fruits from a Turkish collection. Among a total of 80 Bt isolates, 18 of them were found carrying a vip3 gene (in 23% of total), which were further selected. Insecticidal activity of spore/crystal mixtures and their supernatants showed that some of the Bt isolates had significantly more toxicity against some lepidopteran species than the HD1 reference strain. Five isolate…

0301 basic medicineTurkeyProtein ExpressionBacillus Thuringiensislcsh:MedicineArtificial Gene Amplification and ExtensionBacillusProtein SequencingMothsToxicologyPathology and Laboratory MedicinePolymerase Chain ReactionDatabase and Informatics MethodsBacillus thuringiensisMedicine and Health SciencesToxinslcsh:ScienceMaterialsSoil MicrobiologyMultidisciplinaryBacterial PathogensMedical MicrobiologyPhysical SciencesPathogensSequence AnalysisResearch ArticleSequence analysisBioinformatics030106 microbiologyBacterial ToxinsMaterials ScienceToxic AgentsSequence DatabasesBiologySpodopteraHelicoverpa armigeraResearch and Analysis MethodsCrystalsMicrobiologyMicrobiology03 medical and health sciencesBacterial ProteinsGene Expression and Vector TechniquesAnimalsPest Control BiologicalMolecular Biology TechniquesSequencing TechniquesGeneMolecular BiologyMicrobial PathogensPlant DiseasesGenetic diversityMolecular Biology Assays and Analysis TechniquesToxicityBacterialcsh:RfungiOrganismsBiology and Life Sciencesbiology.organism_classificationFicusSporePlant Leaves030104 developmental biologyBiological DatabasesCry1AcSusceptibilityFruitlcsh:QPloS one
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Survival of two strains of Phthorimaea operculella (Lepidoptera: Gelechiidae) reared on transgenic potatoes expressing a Bacillus thuringiensis cryst…

1998

[Otros] Survie de deux souches de Phthorimaea operculella (Lepidoptera : Gelechiidae) élevées sur des pommes de terre transgéniques exprimant la protéine CrylAb de Bacillus thuringiensis. Deux populations de Phthorimaea operculella (Zeller), l'une supposée résistante au DipelTM (une préparation commerciale de delta-endotoxines de Bacillus thuringiensis) et l'autre sensible, ont été cultivées sur quatre cultivars de pomme de terre, deux transgéniques de première génération, exprimant la protéine CrylAb de Bacillus thuringiensis, et deux non transformés. La population de papillons considérée comme résistante a présenté une mortalité inférieure à celle de l'autre population, mais n'était pas v…

Pesticide resistancePopulationBacillus thuringiensisGenetically modified cropsLepidoptera genitaliaBacillus thuringiensisBotanyCry1AbeducationComputingMilieux_MISCELLANEOUSTransgenic potatoes[SDV.SA] Life Sciences [q-bio]/Agricultural scienceseducation.field_of_studybiologyfungifood and beveragesbiology.organism_classificationGelechiidaePommes de terre transgéniquesPthorimaea operculellaPhthorimaea operculella[SDV.EE] Life Sciences [q-bio]/Ecology environmentHorticultureAgronomy and Crop ScienceSolanaceaeAgronomie
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Proteolytic Processing ofBacillus thuringiensisCryIIIA Toxin and Specific Binding to Brush-Border Membrane Vesicles ofLeptinotarsa decemlineata(Color…

1996

Abstract The mode of action of Bacillus thuringiensis insecticidal proteins in lepidopteran insects is known to involve five steps: ingestion, solubilization, protease activation, binding to midgut membrane receptors, and disruption of the intestinal membrane. Two of these steps, protease activation and binding to midgut membrane receptors, have been analyzed in the major potato pest, the coleoptera Leptinotarsa decemlineata (Colorado potato beetle). Unlike recently proposed, after treatment of the coleopteran-specific B. thuringiensis toxin CryIIIA with gut content from the Colorado potato beetle, a 42-kDa processing polypeptide has been identified. The study of binding to midgut membrane …

ProteasesChymotrypsinProteasebiologyHealth Toxicology and Mutagenesismedicine.medical_treatmentfungiColorado potato beetleBiological pest controlfood and beveragesMidgutGeneral Medicinebiology.organism_classificationBiochemistryBacillus thuringiensisbiology.proteinmedicineBinding siteAgronomy and Crop SciencePesticide Biochemistry and Physiology
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