Search results for "Bacillus thuringiensi"

showing 10 items of 213 documents

Genomics and Proteomics Analyses Revealed Novel Candidate Pesticidal Proteins in a Lepidopteran-Toxic Bacillus thuringiensis Strain

2020

Discovery and identification of novel insecticidal proteins in Bacillus thuringiensis (Bt) strains are of crucial importance for efficient biological control of pests and better management of insect resistance. In this study, the Bt strain KhF, toxic for Plodia interpunctella and Grapholita molesta larvae, underwent genomics and proteomics analyses to achieve a better understanding of the bases of its pathogenicity. The whole-genome sequencing results revealed that the KhF strain contained nine coding sequences with homologies to Bt insecticidal genes. The lepidopteran toxic mixture of spores and crystals of this Bt strain was subjected to liquid chromatography and tandem mass spectrometry …

Health Toxicology and MutagenesisXpp proteinslcsh:MedicineMpp proteinsGenomicsinsect bioassayToxicologymedicine.disease_causeProteomicsTandem mass spectrometryDNA sequencing03 medical and health sciencesBacillus thuringiensismedicinecharacterizationLC-MS/MSGene<i>Plodia interpunctella</i>030304 developmental biology0303 health sciencesStrain (chemistry)biology030306 microbiologyToxinPharmacology. Therapylcsh:Rfungibiology.organism_classificationgenome sequencingBiochemistry<i>Grapholita molesta</i>Toxins
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Differences in the midgut proteolytic activity of twoHeliothis virescens strains, one susceptible and one resistant toBacillus thuringiensis toxins

1996

The development of resistance to Bacillus thuringiensis toxic proteins is a growing concern because it could threaten both conventional and gene transfer use of this environmentally safe biological insecticide. The most common mechanism of resistance involves changes in binding affinity of toxin receptors in the insect midgut membrane. This has not been the case in Heliothis virescens. We have investigated changes in midgut proteolytic activity as a possibility to explain the resistance observed in this insect species. We have developed an improvement of known methods to demonstrate proteolytic activity in crude extracts. Using this method we have found differences in the proteolytic activi…

Heliothis virescensbiologyStrain (chemistry)PhysiologyToxinmedia_common.quotation_subjectfungiMidgutGeneral MedicineInsectbiology.organism_classificationmedicine.disease_causeBiochemistryIn vitroMicrobiologyInsect ScienceBacillus thuringiensismedicineReceptormedia_commonArchives of Insect Biochemistry and Physiology
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Hemocytes of Rhynchophorus ferrugineus (Olivier)(Coleoptera: Curculionidae) and their response to Saccharomyces cerevisiae and Bacillus thuringiensis

2011

Originally from tropical Asia, the Red Palm Weevil (RPW Rhynchophorus ferrugineus (Olivier) is the most dangerous and deadly pest of many palm trees, and there have been reports of its recent detection in France, Greece and Italy. At present, emphasis is on the development of integrated pest management based on biological control rather than on chemical insecticides, however the success of both systems is often insufficient. In this regard, RPW appears to be one pest that is very difficult to control. Thus inves- tigations into the natural defences of this curculionid are advisable. RPW hemocytes, the main immuno- competent cells in the insect, are described for the first time. We identifie…

HemocytesRed Palm Weevil Infection Insect immunity Hemolymph Biological controlBacillus thuringiensisBiological pest controlSettore BIO/05 - ZoologiaSaccharomyces cerevisiaeBiologyMicrobiologyPhagocytosisHemolymphBacillus thuringiensisBotanyHemolymphAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsLarvaWeevilfungibiology.organism_classificationBlood Cell CountBiopesticideRhynchophorusSettore AGR/11 - Entomologia Generale E ApplicataLarvaHost-Pathogen InteractionsWeevilsPEST analysis
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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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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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Characterisation of the structure-function relationship of the Bacillus thuringiensis Vip3A insecticidal proteins

2017

L'agricultura contemporània exigeix cada cop més un ús sostenible d’agroquímics per tal de reduir l'impacte ambiental i el risc per la salut del consumidor. Alguns bacteris entomopatògens produeixen proteïnes insecticides que s'acumulen en cossos d'inclusió o cristalls paraesporales (com ara les proteïnes Cry i Cyt), així com proteïnes insecticides que són secretades al medi de cultiu. Entre les últimes, hi ha les proteïnes Vip, que es divideixen en quatre famílies d'acord amb la seva identitat d'aminoàcids. Les proteïnes Vip1 i Vip2 actuen com toxines binàries i són tòxiques per a alguns coleòpters i hemípters. Per la família de les Vip4, que és l’última família de proteïnes Vip descoberta…

Insecticidal proteinsBiological controlBacillus thuringiensisProtein structureProtein functionIPMVip3A proteins
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Domain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pests

2020

The bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested…

InsecticidesAsiaInsectaHealth Toxicology and Mutagenesismedicine.medical_treatmentBacillus thuringiensislcsh:MedicineSpodopteraToxicologyArticleLethal Dose 5003 medical and health sciencesHelicoverpa armigeraBacterial ProteinsProtein DomainsBacillus thuringiensismedicineAnimalsSpodoptera littoralisPest Control Biological030304 developmental biologychemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyProtein Stabilitylcsh:RfungiSpodoptera spp.Ostrinia furnacalisSouth Americabiology.organism_classificationFusion proteinAnticarsia gemmatalisAmino acidEuropeAnticarsia gemmatalisspodoptera spp. helicoverpa armigeraBiochemistrychemistryAfricaNorth AmericaMamestra brassicaeOstrinia furnacalis
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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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