Search results for "Bacillus thuringiensi"

showing 10 items of 213 documents

Insecticidal Activity and Synergistic Combinations of Ten Different Bt Toxins against Mythimna separata (Walker)

2018

The oriental armyworm (OAW), Mythimna separata (Walker), is a destructive pest of agricultural crops in Asia and Australia. Commercialized Bt crops have performed very well against their target pests

0301 basic medicineInsecticidesHealth Toxicology and MutagenesisBacterial ToxinsBacillus thuringiensislcsh:MedicineVip3 proteinMothsToxicologymedicine.disease_causeArticleMicrobiology03 medical and health sciencesMythimna separataBacillus thuringiensis<i>Bacillus thuringiensis</i>medicineAnimalsBioassayPotencyCry proteinbiologyToxinlcsh:Rfungifood and beveragesDrug Synergismbiology.organism_classification030104 developmental biologyCry1AcLarvaoriental armywormPEST analysisBacteriaToxins
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Functional significance of membrane associated proteolysis in the toxicity of Bacillus thuringiensis Cry3Aa toxin against Colorado potato beetle.

2012

Abstract Bacillus thuringiensis Cry toxins are widely used as biocontrol agents in bioinsecticides and transgenic plants. In the three domain-Cry toxins, domain II has been identified as an important determinant of their highly specific activity against insects. In this work, we assessed the role in membrane associated proteolysis and toxicity in Colorado potato beetle (CPB) of a previously reported ADAM recognition motif present in Cry3Aa toxin domain II. We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 344, 346, 347, 351 and 353 of the ADAM recognition motif in Cry3Aa toxin. Cry3Aa toxin mutants displayed decreased toxicity when comp…

ProteasesColoradoProteolysisMutantBacillus thuringiensisToxicologymedicine.disease_causeMicrobiologyHemolysin ProteinsRecognition sequenceBacterial ProteinsBacillus thuringiensismedicineAnimalsAmino Acid SequencePest Control BiologicalCells Culturedbiologymedicine.diagnostic_testBacillus thuringiensis ToxinsMicrovilliToxinfungiColorado potato beetleWild typeSequence Analysis DNAbiology.organism_classificationColeopteraEndotoxinsBiochemistryProteolysisMutagenesis Site-DirectedToxicon : official journal of the International Society on Toxinology
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Mode of action of Bacillus thuringiensis PS86Q3 strain in hymenopteran forest pests

2001

The mode of action of Cry toxins has been described principally in lepidopteran insects as a multistep process. In this work we describe the mode of action of a Cry toxin active in the common pine sawfly Diprion pini (Hymenoptera, Diprionidae), considered a major forest pest in Europe. Strain PS86Q3 contains a long bipyramidal crystal composed of five major proteins. The N-terminal sequence shows that the 155 kDa protein corresponds to Cry5B toxin and the other proteins belong to the Cry5A subgroup. PCR analysis indicates the presence of cry5Ac and cry5Ba genes, suggesting that Cry5A protein should be Cry5Ac. Activation of protoxins with trypsin or with midgut content from D. pini and Cepha…

DiprionidaeBacterial ToxinsBacillus thuringiensisBiotinmedicine.disease_causeBiochemistryMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsMode of actionMolecular BiologyBacillus thuringiensis ToxinsbiologyToxinfungiMidgutTrypsinbiology.organism_classificationHymenopteraEndotoxinsEnzyme ActivationSawflyLarvaInsect ScienceDiprion pinimedicine.drugInsect Biochemistry and Molecular Biology
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Lyophilization of lepidopteran midguts: a preserving method for Bacillus thuringiensis toxin binding studies

2004

Binding assays with brush border membrane vesicles (BBMV) from insect midguts are commonly used in the study of the interactions between Bacillus thuringiensis Cry toxins and their receptors. Collaboration between laboratories often require that frozen insect samples are sent in dry ice. Because of customs restrictions and delays, sample thawing is always a risk and often the biological material becomes ruined during shipping. We have tested lyophilization as an alternative method for preserving insect midguts for binding studies with B. thuringiensis Cry toxins. For this purpose, BBMV were prepared from both frozen and lyophilized midguts from three lepidopteran species: Spodoptera exigua,…

Brush borderBacillus thuringiensisReceptors Cell SurfaceHelicoverpa armigeraSpodopteramedicine.disease_causeHost-Parasite InteractionsMicrobiologyBacterial ProteinsBacillus thuringiensisExiguamedicineAnimalsBinding sitePest Control BiologicalEcology Evolution Behavior and SystematicsCryopreservationMicrovillibiologyToxinfungibiology.organism_classificationLepidopteraFreeze DryingBiochemistryManduca sextaInsect ProteinsDigestive SystemJournal of Invertebrate Pathology
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Biochemistry and genetics of insect resistance toBacillus thuringiensisinsecticidal crystal proteins

1995

Current knowledge of biochemical mechanisms of insect resistance to Bacillus thuringiensis is reviewed. Available information on resistance inheritance and on patterns of cross-resistance is included. Modification of the binding sites for B. thuringiensis insecticidal crystal proteins has been found in different populations of three insect species. This resistance mechanism seems to be inherited as a single recessive or partially recessive major gene, and the resistance levels reached are high. Altered proteolytic processing of B. thuringiensis crystal proteins has been suggested to be involved in one case of resistance. From the available data it seems that binding site modification is the…

GeneticsBacillaceaebiologymedia_common.quotation_subjectInsectbiology.organism_classificationMicrobiologyMajor geneBacillalesBiochemistryBacillus thuringiensisGeneticsBinding siteMolecular BiologyGeneBacteriamedia_commonFEMS Microbiology Letters
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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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Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua

2021

The ATP binding cassette (ABC) transporters are membrane proteins that can act as putative receptors for Cry proteins from Bacillus thuringiensis (Bt) in the midgut of different insects. For the beet armyworm, Spodoptera exigua, ABCC2 and ABCC3 have been found to interact with Cry1A proteins, the main insecticidal proteins used in Bt crops, as well as Bt-based pesticides. The ABCC2 has shown to have specific binding towards Cry1Ac and is involved in the toxic process of Cry1A proteins, but the role of this transporter and how it relates with the Cry1A proteins is still unknown. Here, we have characterized the interactions between the SeABCC2 and the main proteins that bind to the receptor. …

0301 basic medicineCell SurvivalBacillus thuringiensisATP-binding cassette transporterSpodopteraSpodopteraBiochemistryHemolysin Proteins03 medical and health sciences0302 clinical medicineBacterial ProteinsProtein DomainsBacillus thuringiensisSf9 CellsAnimalsBinding siteReceptorMolecular BiologyBinding SitesBacillus thuringiensis ToxinsbiologyChemistryfungifood and beveragesTransporterCell Biologybiology.organism_classificationMultidrug Resistance-Associated Protein 2Endotoxins030104 developmental biologyMembrane proteinCry1AcBiochemistryMutationInsect ProteinsMultidrug Resistance-Associated ProteinsProtein Multimerization030217 neurology & neurosurgeryProtein BindingBiochemical Journal
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Genetic variability of Spodoptera frugiperda Smith (Lepidoptera: Noctuidae) populations from Latin America is associated with variations in susceptib…

2006

ABSTRACT Bacillus thuringiensis strains isolated from Latin American soil samples that showed toxicity against three Spodoptera frugiperda populations from different geographical areas (Mexico, Colombia, and Brazil) were characterized on the basis of their insecticidal activity, crystal morphology, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of parasporal crystals, plasmid profiles, and cry gene content. We found that the different S. frugiperda populations display different susceptibilities to the selected B. thuringiensis strains and also to pure preparations of Cry1B, Cry1C, and Cry1D toxins. Binding assays performed with pure toxin demonstrated that the differences in the …

Bacterial ToxinsBacillus thuringiensisSpodopteraSpodopteraApplied Microbiology and BiotechnologyPolymerase Chain ReactionLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisGenetic variationparasitic diseasesInvertebrate MicrobiologyAnimalsGenetic variabilityPest Control BiologicalSoil MicrobiologyGeneticsGenetic diversityGenetically modified maizeEcologybiologyBacillus thuringiensis ToxinsMicrovillibusiness.industryfungiGenetic Variationbiology.organism_classificationBiotechnologyRandom Amplified Polymorphic DNA TechniqueEndotoxinsLatin AmericaNoctuidaebusinessFood ScienceBiotechnologyApplied and environmental microbiology
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Trans-generational immune priming in the mealworm beetle protects eggs through pathogen-dependent mechanisms imposing no immediate fitness cost for t…

2018

8 pages; International audience; Immune-challenged mothers can improve their offspring immunity through trans-generational immune priming (TGIP). In insects, TGIP endows the offspring with lifetime immunity, including the eggs, which are likely exposed soon after maternal infection. Egg protection may rely on the transfer of maternal immune effectors to the egg or/and the induction of egg immune genes. These respective mechanisms are assumed to have early-life fitness costs of different magnitude for the offspring. We provide evidence in the mealworm beetle Tenebrio molitor that enhanced egg immunity following a maternal immune challenge is achieved by both of these mechanisms but in a path…

0301 basic medicineMealwormOffspringMaternal effectsmedia_common.quotation_subjectHost–pathogen interactionanimal diseasesImmunologyBacillus thuringiensisZoologychemical and pharmacologic phenomenaInsectBiologyEcological immunology03 medical and health sciencesImmune systemImmunity[ SDV.EE.IEO ] Life Sciences [q-bio]/Ecology environment/SymbiosisAnimals[ SDV.IMM ] Life Sciences [q-bio]/ImmunologyArthrobacterTenebrioCells CulturedOvummedia_commonHost-pathogen interactionEcologyHatching[SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE]Maternal effectBacterial Infectionsbiochemical phenomena metabolism and nutritionbiology.organism_classificationBiological EvolutionInvertebrates[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyFitness costs030104 developmental biologyLarvaHost-Pathogen Interactions[SDV.IMM]Life Sciences [q-bio]/ImmunologybacteriaImmunizationGenetic FitnessImmunity Maternally-AcquiredDevelopmental Biology[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/Symbiosis
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Binding Site Alteration Is Responsible for Field-Isolated Resistance to Bacillus thuringiensis Cry2A Insecticidal Proteins in Two Helicoverpa Species

2010

Background Evolution of resistance by target pests is the main threat to the long-term efficacy of crops expressing Bacillus thuringiensis (Bt) insecticidal proteins. Cry2 proteins play a pivotal role in current Bt spray formulations and transgenic crops and they complement Cry1A proteins because of their different mode of action. Their presence is critical in the control of those lepidopteran species, such as Helicoverpa spp., which are not highly susceptible to Cry1A proteins. In Australia, a transgenic variety of cotton expressing Cry1Ac and Cry2Ab (Bollgard II) comprises at least 80% of the total cotton area. Prior to the widespread adoption of Bollgard II, the frequency of alleles conf…

0106 biological sciencesCrops AgriculturalInsecticidesHelicoverpa punctigeraScienceUNESCO::CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología generalBacillus thuringiensisBacterial ProteinGenetically modified cropsHelicoverpa armigera01 natural sciencesMicrobiologyLepidoptera genitaliaInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanyBacillus thuringiensiBiotechnology/Applied MicrobiologyAnimalsMode of actionBiotechnology/Plant BiotechnologyHelicoverpaInsecticide030304 developmental biology0303 health sciencesMultidisciplinaryBinding SitesbiologyAnimalQfungiBinding SiteRbiology.organism_classificationBinding site alterationHelicoverpa speciesLepidoptera010602 entomologyCry1AcBacillus thuringiensis; Binding site alteration; Helicoverpa speciesMedicine:CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología general [UNESCO]Plant Biology/Agricultural BiotechnologyResearch ArticleProtein BindingPLoS ONE
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