Search results for "bacillus thuringiensis"

showing 10 items of 211 documents

Association of Cry1Ac toxin resistance in Helicoverpa zea (Boddie) with increased alkaline phosphatase levels in the midgut lumen.

2012

ABSTRACT Resistance to Bacillus thuringiensis Cry1Ac toxin was characterized in a population of Helicoverpa zea larvae previously shown not to have an alteration in toxin binding as the primary resistance mechanism to this toxin. Cry1Ac-selected larvae (AR1) were resistant to protoxins and toxins of Cry1Ab, Cry1Ac, and the corresponding modified proteins lacking helix α-1 (Cry1AbMod and Cry1AcMod). When comparing brush border membrane vesicles (BBMVs) prepared from susceptible (LC) and AR1 larval midguts, there were only negligible differences in overall Cry1Ac toxin binding, though AR1 had 18% reversible binding, in contrast to LC, in which all binding was irreversible. However, no differe…

Brush borderPopulationBacterial Proteinmedicine.disease_causeApplied Microbiology and BiotechnologyHemolysin ProteinsEndotoxinBacterial ProteinsBacillus thuringiensismedicineInvertebrate MicrobiologyAnimalseducationeducation.field_of_studybiologyEcologyBacillus thuringiensis ToxinsToxinAnimalfungiMidgutHemolysin ProteinLigand (biochemistry)biology.organism_classificationAlkaline PhosphataseEndotoxinsGastrointestinal TractLepidopteraBiochemistryLarvaAlkaline phosphataseHelicoverpa zeaFood ScienceBiotechnologyProtein BindingApplied and environmental microbiology
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In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by 125 I Radiolabeling

2014

ABSTRACT Bacillus thuringiensis vegetative insecticidal proteins (Vip3A) have been recently introduced in important crops as a strategy to delay the emerging resistance to the existing Cry toxins. The mode of action of Vip3A proteins has been studied in Spodoptera frugiperda with the aim of characterizing their binding to the insect midgut. Immunofluorescence histological localization of Vip3Aa in the midgut of intoxicated larvae showed that Vip3Aa bound to the brush border membrane along the entire apical surface. The presence of fluorescence in the cytoplasm of epithelial cells seems to suggest internalization of Vip3Aa or a fragment of it. Successful radiolabeling and optimization of the…

Brush bordermedia_common.quotation_subjectSpodopteraSpodopteraHemolysin ProteinsBinding CompetitiveApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsTrypsinBinding siteInternalizationmedia_commonBinding SitesBacillus thuringiensis ToxinsMicrovilliEcologybiologyfungiEpithelial CellsMidgutHydrogen-Ion Concentrationbiology.organism_classificationEndotoxinsBiochemistryCytoplasmIsotope LabelingLarvaDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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Acute Toxicity Tests with Cadmium, Lead, Sodium Dodecyl Sulfate, and Bacillus thuringiensis on a Temporary Pond Ostracod

2012

A complete assessment of effects of pollutants in the environment requires the use of a wide assemblage of test organisms. Crustaceans have been widely used in aquatic environments, but within this group, ostracods have been overlooked, even though they are one of the commonest groups of animals in temporary waters. Within this framework, static acute toxicity bioassays were conducted with heavy metals Cd and Pb, the surfactant SDS and spores of the bacteria Bacillus thuringiensis var. israeliensis using adult parthenogenetic females of the temporary pond ostracod Heterocypris bosniaca. Experiments were run at 20 °C and in a 12 by 12 h photoperiod. The toxicity tests results are expressed a…

Cadmiumbiologychemistry.chemical_elementAquatic Sciencebiology.organism_classificationCrustaceanAcute toxicitySporeToxicologychemistryBacillus thuringiensisEnvironmental chemistryToxicityBioassayEcology Evolution Behavior and SystematicsEC50International Review of Hydrobiology
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Bacillus thuringiensis Cry1Ac Toxin-Binding and Pore-Forming Activity in Brush Border Membrane Vesicles Prepared from Anterior and Posterior Midgut R…

2008

ABSTRACT It is generally accepted that Bacillus thuringiensis Cry toxins insert into the apical membrane of the larval midgut after binding to specific receptors, and there is evidence that the distribution of binding molecules along the midgut is not uniform. By use of the voltage-sensitive dye DiSC 3 (5) and 125 I-labeled Cry1Ac, we have measured the effect of Cry1Ac in terms of permeabilization capacity and of binding parameters on brush border membrane vesicles (BBMV) prepared from the anterior and the posterior regions of the larval midgut from two insect species, Manduca sexta and Helicoverpa armigera . The permeabilizing activity was significantly higher with BBMV from the posterior …

Cell Membrane PermeabilityBrush bordermedia_common.quotation_subjectBacterial ProteinInsectApplied Microbiology and BiotechnologyIodine RadioisotopeIodine RadioisotopesHemolysin ProteinsEndotoxinBacterial ProteinsManducaBacillus thuringiensisInvertebrate MicrobiologyAnimalsmedia_commonBacillus thuringiensis ToxinsMicrovilliEcologybiologyAnimalVesiclefungiMidgutHemolysin ProteinApical membraneAlkaline Phosphatasebiology.organism_classificationEndotoxinsEnzyme ActivationLepidopteraBiochemistryManduca sextaLarvaPotassiumBiophysicsManducaDigestive SystemProtein BindingFood ScienceBiotechnologyApplied and Environmental Microbiology
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Toxicity and mode of action of Bacillus thuringiensis Cry proteins in the Mediterranean corn borer, Sesamia nonagrioides (Lefebvre)

2006

ABSTRACT Sesamia nonagrioides is one of the most damaging pests of corn in Spain and other Mediterranean countries. Bt corn expressing the Bacillus thuringiensis Cry1Ab toxin is being grown on about 58,000 ha in Spain. Here we studied the mode of action of this Cry protein on S. nonagrioides (binding to specific receptors, stability of binding, and pore formation) and the modes of action of other Cry proteins that were found to be active in this work (Cry1Ac, Cry1Ca, and Cry1Fa). Binding assays were performed with 125 I- or biotin-labeled toxins and larval brush border membrane vesicles (BBMV). Competition experiments indicated that these toxins bind specifically and that Cry1Aa, Cry1Ab, an…

Cell Membrane PermeabilityMembrane permeabilityBacterial ToxinsBacillus thuringiensisSesamia nonagrioidesBacterial ToxinBacterial ProteinZea maysApplied Microbiology and BiotechnologyOstriniaHemolysin ProteinsZea mayBacterial ProteinsEndotoxinBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBacillus thuringiensiBinding siteMode of actionPest Control BiologicalGenetically modified maizeBacillus thuringiensis ToxinsEcologybiologyMicrovilliAnimalfungifood and beveragesHemolysin Proteinbiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraCry1AcBiochemistryLarvaFood ScienceBiotechnology
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Alteration of a Cry1A Shared Binding Site in a Cry1Ab-Selected Colony of Ostrinia furnacalis

2022

The Asian corn borer, Ostrinia furnacalis (Guenée, 1854), is a highly damaging pest in Asia and the Pacific islands, and larvae feed mainly from corn crops. To determine the suitability of Bt-corn technology for the future control of this pest, understanding the potential to develop resistance to Cry1Ab and the basis of cross-resistance to other Cry1 proteins is of great interest. Here, we have explored the binding of Cry1A proteins to brush border membrane vesicles from two O. furnacalis colonies, one susceptible (ACB-BtS) and one laboratory-selected with Cry1Ab (ACB-AbR). The insects developed resistance to Cry1Ab and showed cross-resistance to Cry1Aa, Cry1Ac, and Cry1F. Binding assays wi…

ChinaBinding SitesBacillus thuringiensis ToxinsCry1 toxinsHealth Toxicology and Mutagenesisfungibinding site modelBacillus thuringiensisRfood and beveragespyramid strategyMothsAsian corn borer; <i>Bacillus thuringiensis</i>; Cry1 toxins; binding site model; pyramid strategyToxicologyAsian corn borerZea maysArticleInsecticide ResistanceLarva<i>Bacillus thuringiensis</i>AnimalsMedicinePest Control BiologicalToxins
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Midgut microbiota and host immunocompetence underlie Bacillus thuringiensis killing mechanism

2016

Bacillus thuringiensis is a widely used bacterial entomopathogen producing insecticidal toxins, some of which are expressed in insect-resistant transgenic crops. Surprisingly, the killing mechanism of B. thuringiensis remains controversial. In particular, the importance of the septicemia induced by the host midgut microbiota is still debated as a result of the lack of experimental evidence obtained without drastic manipulation of the midgut and its content. Here this key issue is addressed by RNAi-mediated silencing of an immune gene in a lepidopteran host Spodoptera littoralis, leaving the midgut microbiota unaltered. The resulting cellular immunosuppression was characterized by a reduced …

Crops Agricultural0301 basic medicineHemocytesSerratiaBacillus thuringiensisSpodopteraSerratiaMicrobiologyHemolysin Proteins03 medical and health sciencesBacterial ProteinsInsect-pathogen interactionImmunityBacillus thuringiensisAnimalsPest Control Biologicalbioinsecticide | insect-pathogen interactions | insect biocontrol | pore-forming toxins | immunitySpodoptera littoralisRNA Double-StrandedClostridiumImmunosuppression TherapyPore-forming toxinMultidisciplinaryBacillus thuringiensis ToxinsInsect biocontrolbiologyHost (biology)MicrobiotafungiImmunityMidgutBiological Sciencesbiology.organism_classificationImmunity InnateBioinsecticideEndotoxinsIntestines030104 developmental biologyGene Expression RegulationLarvaPore-forming toxinInsect ProteinsRNA InterferenceImmunocompetenceProceedings of the National Academy of Sciences
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Vip3C, a novel class of vegetative insectidal proteins from Bacillus thuringiensis

2012

Three vip3 genes were identified in two Bacillus thuringiensis Spanish collections. Sequence analysis revealed a novel Vip3 protein class (Vip3C). Preliminary bioassays of larvae from 10 different lepidopteran species indicated that Vip3Ca3 caused more than 70% mortality in four species after 10 days at 4 οg/cm 2. © 2012, American Society for Microbiology.

DNA BacterialBioquímicaSequence analysisMolecular Sequence DataBiotecnologia agrícolaBacillus thuringiensisBiologyApplied Microbiology and BiotechnologyLepidoptera genitaliaBacterial proteinPlagues ControlBacterial ProteinsPhylogeneticsBacillus thuringiensisBotanyPlaguicidesInvertebrate MicrobiologyAnimalsBioassayGenePhylogenyLarvaSequence Homology Amino AcidEcologyfungiSequence Analysis DNAbiology.organism_classificationSurvival AnalysisVip3 genesLepidopteraSpainLarvaProteïnesFood ScienceBiotechnology
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Role of Bacillus thuringiensis Toxin Domains in Toxicity and Receptor Binding in the Diamondback Moth

1999

ABSTRACT The toxic fragment of Bacillus thuringiensis crystal proteins consists of three distinct structural domains. There is evidence that domain I is involved in pore formation and that domain II is involved in receptor binding and specificity. It has been found that, in some cases, domain III is also important in determining specificity. Furthermore, involvement of domain III in binding has also been reported recently. To investigate the role of toxin domains in the diamondback moth ( Plutella xylostella ), we used hybrid toxins with domain III substitutions among Cry1C, Cry1E, and Cry1Ab. Neither Cry1E nor G27 (a hybrid with domains I and II from Cry1E and domain III from Cry1C) was to…

Diamondback mothBacillaceaeEcologyEcologyToxinfungiParasporal bodyBiologybiology.organism_classificationmedicine.disease_causeApplied Microbiology and BiotechnologyBacillalesBiochemistryPlant Research InternationalBacillus thuringiensisInvertebrate MicrobiologymedicineLife ScienceBinding siteBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
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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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