Search results for "Bacillus thuringiensis"

showing 10 items of 211 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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A Genomic and Proteomic Approach to Identify and Quantify the Expressed Bacillus thuringiensis Proteins in the Supernatant and Parasporal Crystal

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_…

0301 basic medicineInsecticidesbiologyInsect pest controlHealth Toxicology and MutagenesisSingle typelcsh:Rcry proteinslcsh:Medicinevip proteinsToxicologybiology.organism_classificationMolecular biologyinsect pest control; crop protection; vip proteins; cry proteins03 medical and health sciences030104 developmental biologyinsect pest controlBacillus thuringiensisGeneProteïnescrop protection
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Susceptibility, mechanisms of response and resistance to Bacillus thuringiensis toxins in Spodoptera spp.

2016

Bioinsecticides based on Bacillus thuringiensis have long been used as an alternative to synthetic insecticides to control insect pests. In this review, we focus on insects of the genus Spodoptera, including relevant polyphagous species that are primary and secondary pests of many crops, and how B. thuringiensis toxins can be used for Spodoptera spp. pest management. We summarize the main findings related to susceptibility, midgut binding specificity, mechanisms of response and resistance of this insect genus to B. thuringiensis toxins.

0301 basic medicineIntegrated pest managementResistance (ecology)media_common.quotation_subjectBacterial ToxinsfungiBacillus thuringiensisfood and beveragesMidgutInsectSpodopteraBiologySpodopterabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciences030104 developmental biologyInsect ScienceBacillus thuringiensisBotanyAnimalsEcology Evolution Behavior and Systematicsmedia_commonCurrent Opinion in Insect Science
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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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Editorial for Special Issue: The Insecticidal Bacterial Toxins in Modern Agriculture.

2017

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0301 basic medicineMicrobial toxinsBacillus thuringiensis Toxinsbusiness.industryHealth Toxicology and Mutagenesislcsh:RBacillus thuringiensislcsh:MedicineBiologyToxicologyPlants Genetically ModifiedBiotechnologyEndotoxins03 medical and health sciencesHemolysin Proteins030104 developmental biologyn/aEditorialBacterial ProteinsAgriculturebusinessPest Control BiologicalEcosystemToxins
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Critical amino acids for the insecticidal activity of Vip3Af from Bacillus thuringiensis: Inference on structural aspects

2018

AbstractVip3 vegetative insecticidal proteins from Bacillus thuringiensis are an important tool for crop protection against caterpillar pests in IPM strategies. While there is wide consensus on their general mode of action, the details of their mode of action are not completely elucidated and their structure remains unknown. In this work the alanine scanning technique was performed on 558 out of the total of 788 amino acids of the Vip3Af1 protein. From the 558 residue substitutions, 19 impaired protein expression and other 19 substitutions severely compromised the insecticidal activity against Spodoptera frugiperda. The latter 19 substitutions mainly clustered in two regions of the protein …

0301 basic medicineModels MolecularAmino Acid MotifsBacillus thuringiensislcsh:MedicineSpodopteraSpodopteraArticle03 medical and health sciencesProtein structureProtein sequencingBacterial ProteinsBacillus thuringiensisAnimalsMode of actionlcsh:Sciencechemistry.chemical_classificationMultidisciplinaryAlaninebiologyProtein Stabilitylcsh:RAlanine scanningbiology.organism_classificationProtein tertiary structureAmino acidProtein Structure TertiaryMolecular Docking Simulation030104 developmental biologychemistryBiochemistryAmino Acid Substitutionlcsh:QScientific Reports
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Artefactual band patterns by SDS-PAGE of the Vip3Af protein in the presence of proteases mask the extremely high stability of this protein.

2018

Abstract Vip3 proteins are secretable proteins from Bacillus thuringiensis with important characteristics for the microbiological control of agricultural pests. The exact details of their mode of action are yet to be disclosed and the crystallographic structure is still unknown. Vip3 proteins are expressed as protoxins that have to be activated by the insect gut proteases. A previous study on the peptidase processing of Vip3Aa revealed that the protoxin produced artefactual band patterns by SDS-PAGE due to the differential stability of this protein and the peptidases to SDS and heating (Bel et al., 2017 Toxins 9:131). To determine whether this phenomenon also applies to other Vip3A proteins…

0301 basic medicineProteases030106 microbiologyBacillus thuringiensisSpodopteraSpodopteraCleavage (embryo)Biochemistry03 medical and health sciencesBacterial ProteinsStructural BiologyBacillus thuringiensismedicineAnimalsMode of actionMolecular BiologyPolyacrylamide gel electrophoresisbiologyChemistryProtein StabilityfungiMidgutGeneral Medicinebiology.organism_classificationTrypsin030104 developmental biologyBiochemistryInsect ProteinsElectrophoresis Polyacrylamide Gelmedicine.drugPeptide HydrolasesInternational journal of biological macromolecules
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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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Analysis of cross-resistance to Vip3 proteins in eight insect colonies, from four insect species, selected for resistance to Bacillus thuringiensis i…

2018

Abstract Bacillus thuringiensis Vip3 proteins are synthesized and secreted during the vegetative growth phase. They are activated by gut proteases, recognize and bind to midgut receptors, form pores and lyse cells. We tested the susceptibility to Vip3Aa and Vip3Ca of Cry1A-, Cry2A-, Dipel- and Vip3-resistant insect colonies from different species to determine whether resistance to other insecticidal proteins confers cross-resistance to Vip3 proteins. As expected, the colonies resistant to Cry1A proteins, Dipel (Helicoverpa armigera, Trichoplusia ni, Ostrinia furnacalis and Plodia interpunctella) or Cry2Ab (H. armigera and T. ni) were not cross-resistant to Vip3 proteins. In contrast, H. arm…

0301 basic medicineProteasesInsectabiologymedia_common.quotation_subjectfungi030106 microbiologyBacillus thuringiensisMidgutInsectHelicoverpa armigerabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsCross-resistancemedia_commonOstrinia furnacalisJournal of Invertebrate Pathology
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Ephestia kuehniella tolerance to Bacillus thuringiensis Cry1Aa is associated with reduced oligomer formation

2016

The basis of the different susceptibility of Ephestia kuehniella to the Cry1Aa and Cry1Ac δ-endotoxins from Bacillus thuringiensis kurstaki BNS3 was studied. Both toxins bound specifically to the BBMV of E. kuehniella. The result of the ligand blot showed that Cry1Ac bound to three putative receptors of about 100, 65 and 80 kDa and Cry1Aa interacted only with a 100 kDa protein. Pronase digestion of the BBMV-bound toxins was used to analyze the toxin insertion. Both toxins inserted into the BBMV as monomers however, a 14 kDa peptide of α4-α5 which correspond to the oligomeric form of this peptide was detected in case of Cry1Ac only. Analysis of the in vitro oligomerisation of these toxins in…

0301 basic medicineProtein ConformationBacillus thuringiensisBiophysicsPeptidemedicine.disease_causeBiochemistryOligomerHemolysin Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsBacillus thuringiensismedicineAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis Toxins030102 biochemistry & molecular biologybiologyToxinfungiCell BiologyLigand (biochemistry)biology.organism_classificationEndotoxinsLepidopteraBlot030104 developmental biologyBiochemistryCry1AcchemistryProtein MultimerizationBiochemical and Biophysical Research Communications
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