Search results for "Bacillus thuringiensis"

showing 10 items of 211 documents

ABCC transporters mediate insect resistance to multiple Bt toxins revealed by bulk segregant analysis

2014

[EN] Background: Relatively recent evidence indicates that ABCC2 transporters play a main role in the mode of action of Bacillus thuringiensis (Bt) Cry1A-type proteins. Mapping of major Cry1A resistance genes has linked resistance to the ABCC2 locus in Heliothis virescens, Plutella xylostella, Trichoplusia ni and Bombyx mori, and mutations in this gene have been found in three of these Bt-resistant strains. Results: We have used a colony of Spodoptera exigua (Xen-R) highly resistant to a Bt commercial bioinsecticide to identify regions in the S. exigua genome containing loci for major resistance genes by using bulk segregant analysis (BSA). Results reveal a region containing three genes fro…

MalePhysiologyGenes InsectPlant ScienceBt resistanceInsecticide ResistanceHemolysin ProteinsStructural BiologyBacillus thuringiensisChromosome SegregationPhylogenyGeneticsbiologyAgricultural and Biological Sciences(all)LarvaFemaleGeneral Agricultural and Biological SciencesBiotechnologyResearch ArticleMolecular Sequence DataBacillus thuringiensisSpodopteraSpodopteraABCC2 transporterPolymorphism Single NucleotideGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsExiguaAnimalsAmino Acid SequenceGeneEcology Evolution Behavior and SystematicsCrosses GeneticBombyxBacillus thuringiensis ToxinsBiochemistry Genetics and Molecular Biology(all)Gene Expression ProfilingfungiWild typeCell BiologySequence Analysis DNAbiology.organism_classificationBombyxMolecular biologyEndotoxinsKineticsGENETICACry1AcMembrane proteinATP-Binding Cassette TransportersCry toxinsDevelopmental Biology
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The Independent Biological Activity of Bacillus thuringiensis Cry23Aa Protein Against Cylas puncticollis

2020

The Cry23Aa/Cry37Aa proteins from Bacillus thuringiensis (Bt) have been described toxic to Cylas puncticollis larvae. In general, it is believed that Cry23Aa and Cry37Aa act jointly to exert the insecticidal activity, while there is no evidence of their toxicity individually. Therefore, in the present study, the contribution of each protein in the insecticidal activity toward C. puncticollis larvae has been assessed. The results showed that both proteins were toxic for C. puncticollis larvae when tested individually. Contrary to what was claimed previously, our results suggest that the presence of both proteins is not necessary to exert toxicity against C. puncticollis larvae. Also, the bin…

Microbiology (medical)Agriculture and Food SciencesSWEET-POTATO WEEVILlcsh:QR1-502sweet potato weevilsbinary toxinMicrobiologylcsh:Microbiology03 medical and health sciencesmode of actioninsecticidal proteinsBacillus thuringiensisBioassayCry37AaBinding siteSPHAERICUS TOXINMode of action030304 developmental biologybinding assay0303 health sciencesPore-forming toxinLarvabiology030306 microbiologyCRYSTAL PROTEINCOMPONENTSfungiMidgutBiological activityBORDER MEMBRANE-VESICLESENTOMOPATHOGENIC FUNGIbiology.organism_classificationEFFICACYBiochemistrybioassayCOLEOPTERABRUNNEUSRESISTANCEFrontiers in Microbiology
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Characterization ofBacillus thuringiensisisolated from infections in burn wounds

1997

Four strains of Bacillus thuringiensis were isolated from infections in burn wounds and from water used in the treatment of burn wounds. The strains produced large parasporal inclusion bodies composed of 141, 83, and 81 kDa protoxins. The four strains were tested for insecticidal activity against larvae of Pieris brassicae and Aedes aegypti but showed no activity; Vero cell assays for the production of enterotoxins were also negative. Attempts to classify the strains according to flagellar H-serotype showed them all to be non-flagellated. Apart from two occupational health accidents that occurred during the handling of highly concentrated B. thuringiensis fluids, this is the first report of…

Microbiology (medical)Bacterial ToxinsImmunologyBacillus thuringiensisBacillus cereusAedes aegyptiEnterotoxinMicrobiologyMicrobiologyHemolysin ProteinsBacterial ProteinsAedesBacillus thuringiensisChlorocebus aethiopsAnimalsHumansImmunology and AllergyVero CellsPieris brassicaeBacillus thuringiensis Toxinsbiologybacillus thurigiensisinfectionsfungiGeneral Medicinebiology.organism_classificationBacillalesVirologyEndotoxinsInfectious DiseasesWound InfectionVero cellBurnsButterfliesBacteriaFEMS Immunology & Medical Microbiology
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Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis

2020

9 p.-5 fig.

Models Molecular0301 basic medicineProteasesBiologiaMolecular biologymedicine.medical_treatmentScienceAmino Acid MotifsBacillus thuringiensisGeneral Physics and Astronomy02 engineering and technologyGenetically modified cropsBiotecnologiaArticleProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesBacterial ProteinsProtein DomainsTetramerBacillus thuringiensisElectron microscopymedicineTrypsinlcsh:ScienceMultidisciplinaryProteasebiologyChemistryQfungifood and beveragesMidgutGeneral Chemistry021001 nanoscience & nanotechnologybiology.organism_classification030104 developmental biologyStructural biologyBiochemistrylcsh:QStructural biology0210 nano-technologyProteïnesFunction (biology)
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Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
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Proteome response of Tribolium castaneum larvae to Bacillus thuringiensis toxin producing strains.

2012

Susceptibility of Tribolium castaneum (Tc) larvae was determined against spore-crystal mixtures of five coleopteran specific and one lepidopteran specific Bacillus thuringiensis Cry toxin producing strains and those containing the structurally unrelated Cry3Ba and Cry23Aa/Cry37Aa proteins were found toxic (LC(50) values 13.53 and 6.30 µg spore-crystal mixture/µL flour disc, respectively). Using iTRAQ combined with LC-MS/MS allowed the discovery of seven novel differentially expressed proteins in early response of Tc larvae to the two active spore-crystal mixtures. Proteins showing a statistically significant change in treated larvae compared to non-intoxicated larvae fell into two major cat…

Models MolecularProteomicsProteomeTranscription GeneticOdorant bindingProtein ConformationApplied Microbiologylcsh:MedicinePathogenesismedicine.disease_causeReceptors OdorantBiochemistryProtein structureBacillus thuringiensislcsh:SciencePhylogenyTriboliumMultidisciplinaryImmune System ProteinsSpectrometric Identification of ProteinsbiologyChemosensory proteinAgricultureHost-Pathogen InteractionLarvaHost-Pathogen InteractionsInsect ProteinsResearch Articleanimal structuresProtein subunitLipoproteinsBacterial ToxinsMolecular Sequence DataBacillus thuringiensisMicrobiologyBacterial ProteinsRibosomal proteinMicrobial ControlDefense ProteinsmedicineAnimalsAmino Acid SequencePesticidesBiologyToxinfungilcsh:RProteinsbiology.organism_classificationMolecular biologyApolipoproteinsOdorant-binding proteinbiology.proteinlcsh:QPest ControlSequence AlignmentZoologyEntomologyProtein AbundancePLoS ONE
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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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Biochemistry and genetics of insect resistance to Bacillus thuringiensis.

2001

▪ Abstract  Bacillus thuringiensis (Bt) is a valuable source of insecticidal proteins for use in conventional sprayable formulations and in transgenic crops, and it is the most promising alternative to synthetic insecticides. However, evolution of resistance in insect populations is a serious threat to this technology. So far, only one insect species has evolved significant levels of resistance in the field, but laboratory selection experiments have shown the high potential of other species to evolve resistance against Bt. We have reviewed the current knowledge on the biochemical mechanisms and genetics of resistance to Bt products and insecticidal crystal proteins. The understanding of th…

Pesticide resistanceInsectamedia_common.quotation_subjectBacillus thuringiensisInsectGenetically modified cropsBiologyInsecticide ResistanceBacillus thuringiensisAnimalsInsecticidal crystal proteinsPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commonGeneticsResistance (ecology)business.industryDipterafungiPest controlbiology.organism_classificationBiotechnologyColeopteraLepidopteraCry1AcInsect SciencebusinessAnnual review of entomology
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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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A new gene superfamily of pathogen-response (repat) genes in Lepidoptera: Classification and expression analysis

2012

Repat (REsponse to PAThogens) genes were first identified in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae) in response to Bacillus thuringiensis and baculovirus exposure. Since then, additional repat gene homologs have been identified in different studies. In this study the comprehensive larval transcriptome from S. exigua was analyzed for the presence of novel repat-homolog sequences. These analyses revealed the presence of at least 46 repat genes in S. exigua, establishing a new gene superfamily in this species. Phylogenetic analysis and studies of conserved motifs in these hypothetical proteins have allowed their classification in two main classes, αREPAT and βREPAT. Studies o…

PhysiologyBacillus thuringiensisGenes InsectSpodopteradigestive systemBiochemistryTranscriptomeHemolysin ProteinsBacterial ProteinsBacillus thuringiensisGene expressionExiguaAnimalsMolecular BiologyGeneGeneticsBacillus thuringiensis ToxinsbiologyGene Expression ProfilingStem CellsfungiMidgutbiology.organism_classificationMolecular biologyEndotoxinsIntestinesLepidopteraGene expression profilingLarvaMetagenomeComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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