Search results for "Bacillus thuringiensis Toxins"

showing 10 items of 90 documents

Prohibitin, an essential protein for Colorado potato beetle larval viability, is relevant to Bacillus thuringiensis Cry3Aa toxicity

2013

Bacillus thuringienesis (Bt) Cry toxins constitute the most extensively used environmentally safe biopesticide and their mode of action relies on the interaction of the toxins with membrane proteins in the midgut of susceptible insects that mediate toxicity and insect specificity. Therefore, identification of Bt Cry toxin interacting proteins in the midgut of target insects and understanding their role in toxicity is of great interest to exploit their insecticidal action. Using ligand blot, we demonstrated that Bt Cry3Aa toxin bound to a 30kDa protein in Colorado potato beetle (CPB) larval midgut membrane, identified by sequence homology as prohibitin-1 protein. Prohibitins comprise a highl…

ProteasesHealth Toxicology and MutagenesisBiologymedicine.disease_causeHemolysin ProteinsBacterial ProteinsRNA interferenceBacillus thuringiensisProhibitinsmedicineAnimalsProhibitinBinding siteMode of actionSolanum tuberosumBacillus thuringiensis ToxinsToxinfungiGeneral Medicinebiology.organism_classificationMolecular biologyColeopteraEndotoxinsRepressor ProteinsMembrane proteinBiochemistryLarvaAgronomy and Crop SciencePesticide Biochemistry and Physiology
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Unraveling the Composition of Insecticidal Crystal Proteins in Bacillus thuringiensis: a Proteomics Approach.

2020

ABSTRACT Bacillus thuringiensis (Bt) is the most widely used active ingredient for biological insecticides. The composition of δ-endotoxins (Cry and Cyt proteins) in the parasporal crystal determines the toxicity profile of each Bt strain. However, a reliable method for their identification and quantification has not been available, due to the high sequence identity of the genes that encode the δ-endotoxins and the toxins themselves. Here, we have developed an accurate and reproducible mass spectrometry-based method (liquid chromatography-tandem mass spectrometry-multiple reaction monitoring [LC-MS/MS-MRM]) using isotopically labeled proteotypic peptides for each protein in a particular mix…

ProteomicsInsecticidesProteomeQuantitative proteomicsBacillus thuringiensisProteomics01 natural sciencesApplied Microbiology and Biotechnology03 medical and health sciencesBiosafetyHemolysin ProteinsBacterial ProteinsTandem Mass SpectrometryBacillus thuringiensisInvertebrate Microbiology030304 developmental biologyPhytosanitary certificationActive ingredient0303 health sciencesChromatographyEcologybiologyBacillus thuringiensis ToxinsChemistry010401 analytical chemistrybiology.organism_classification0104 chemical sciencesEndotoxinsComposition (visual arts)FermentationFood ScienceBiotechnologyChromatography LiquidApplied and environmental microbiology
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Characterization ofBacillus thuringiensisserovarbolivia(serotype H63), a novel serovar isolated from the Bolivian high valleys

1999

The type strain Bacillus thuringiensis var. bolivia (serotype H63), isolated from the Bolivian high valleys, has been characterized at different levels. Its parasporal crystal has an unusual shape and it is composed of a protein of 155 kDa which shows two bands of 75 and 80 kDa after activation. Analysis by PCR shows the presence of cry1 genes, and amplification with specific primers gave products for cry1 E, cry1 D, cry4 A and cry4 B with sizes different to those expected. Immunoblotting tests showed positive reaction for Cry1 E, Cry3 A, Cry4 A and Cry11 A crystal proteins. The plasmid pattern revealed two large and two small plasmids. Toxicity tests were performed against 14 insects and a…

SerotypeBoliviaBacterial ToxinsBlotting WesternBacillus thuringiensisApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsPlasmidBacterial ProteinsBacillus thuringiensisTrichoplusiaAnimalsBacillaceaeBacillus thuringiensis ToxinsbiologyStrain (chemistry)fungiParasporal bodybiology.organism_classificationBacillalesColeopteraEndotoxinsLarvaMicroscopy Electron ScanningElectrophoresis Polyacrylamide GelPlasmidsLetters in Applied Microbiology
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Characterization of Bacillus thuringiensis ser. balearica (Serotype H48) and ser. navarrensis (serotype H50): two novel serovars isolated in Spain.

2000

The novel strains of Bacillus thuringiensis PM9 and NA69, isolated from soil samples in Spain, were classified and characterized in terms of their crystal proteins, plasmid profile, cry genes content, and their toxicological properties against several species of Lepidoptera, Coleoptera, and Diptera. Both strains share morphological and biochemical characteristics with previously described B. thuringiensis strains, although their unique H antigens identify them as two new serotypes. Two new serovar names, B. thuringiensis serovar balearica (H serotype 48) and B. thuringiensis serovar navarrensis (H serotype 50) are proposed for the type strains PM9 and NA69, respectively.

SerotypeInsectaBacterial ToxinsImmunoblottingBacillus thuringiensisH antigenApplied Microbiology and BiotechnologyMicrobiologyPolymerase Chain ReactionMicrobiologyLepidoptera genitaliaHemolysin ProteinsPlasmidBacterial ProteinsBacillus thuringiensisAnimalsTypingSerotypingPest Control BiologicalSoil MicrobiologyInclusion BodiesAntigens BacterialBacillaceaebiologyBacillus thuringiensis ToxinsfungiGeneral Medicinebiology.organism_classificationBacillalesBacterial Typing TechniquesEndotoxinsElectrophoresis Polyacrylamide GelPlasmidsCurrent microbiology
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Tribolium castaneum immune defense genes are differentially expressed in response to Bacillus thuringiensis toxins sharing common receptor molecules …

2015

In Tribolium castaneum larvae we have demonstrated by RNA interference knockdown that the Bacillus thuringiensis Cry3Ba toxin receptors Cadherin-like and Sodium solute symporter proteins are also functional receptors of the less active Cry3Aa toxin. Differences in susceptibility to B. thuringiensis infection might not only rely on toxin-receptor interaction but also on host defense mechanisms. We compared the expression of the immune related genes encoding Apolipophorin-III and two antimicrobial peptides, Defensin3 and Defensin2 after B. thuringiensis challenge. All three genes were up-regulated following Cry3Ba spore-crystal intoxication whereas only Defensins gene expression was induced u…

Staphylococcus aureusImmunologyAntimicrobial peptidesBacterial ToxinsMolecular Sequence DataBacillus thuringiensisBiologymedicine.disease_causeMicrobiologyDefensinsHemolysin ProteinsImmune systemBacterial ProteinsRNA interferenceBacillus thuringiensisGene expressionCandida albicansmedicineEscherichia coliAnimalsAmino Acid SequenceRNA Small InterferingDefensinTriboliumInnate immune systemBacillus thuringiensis ToxinsSymportersToxinfungibiology.organism_classificationAnti-Bacterial AgentsEndotoxinsApolipoproteinsLarvaInsect ProteinsRNA InterferenceDevelopmental BiologyDevelopmental and comparative immunology
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Potential of the Bacillus thuringiensis Toxin Reservoir for the Control of Lobesia botrana (Lepidoptera: Tortricidae), a Major Pest of Grape Plants▿

2006

ABSTRACT The potential of Bacillus thuringiensis Cry proteins to control the grape pest Lobesia botrana was explored by testing first-instar larvae with Cry proteins belonging to the Cry1, Cry2, and Cry9 groups selected for their documented activities against Lepidoptera. Cry9Ca, a toxin from B. thuringiensis , was the protein most toxic to L. botrana larvae, followed in decreasing order by Cry2Ab, Cry1Ab, Cry2Aa, and Cry1Ia7, with 50% lethal concentration values of 0.09, 0.1, 1.4, 3.2, and 8.5 μg/ml of diet, respectively. In contrast, Cry1Fa and Cry1JA were not active at the assayed concentration (100 μg/ml). In vitro binding and competition experiments showed that none of the toxins teste…

Tortricidaeanimal structuresBacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsmedicine.disease_causeLobesia botranaApplied Microbiology and BiotechnologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsLobesia botranaBacillus thuringiensisBotanymedicineInvertebrate MicrobiologyAnimalsVitisPest Control BiologicalCry proteinsPlant DiseasesEcologybiologyBacillus thuringiensis ToxinsToxinbusiness.industryfungiPest controlfood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticultureLarvaPEST analysisbusinessFood ScienceBiotechnology
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Unshared binding sites for Bacillus thuringiensis Cry3Aa and Cry3Ca proteins in the weevil Cylas puncticollis (Brentidae)

2016

Bacillus thuringiensis Cry3Aa and Cry3Ca proteins have been reported to be toxic against the African sweetpotato pest Cylas puncticollis. In the present work, the binding sites of these proteins in C. puncticollis brush border vesicles suggest the occurrence of different binding sites, but only one of them is shared. Our results suggest that pest resistance mediated by alteration of the shared Cry-receptor binding site might not render both Cry proteins ineffective.

endocrine systemAfrican sweetpotato weevilBacillus thuringiensis ToxinsShort CommunicationBinding sitesInsect controlfungiBacillus thuringiensisToxicologyBinding CompetitiveInsect resistance managementEndotoxinsHemolysin ProteinsInsecticidal proteinsBacterial ProteinsAnimalsWeevilsToxicon
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Extent of variation of the Bacillus thuringiensis toxin reservoir: the case of the geranium bronze, Cacyreus marshalli butler (Lepidoptera: Lycaenida…

2002

ABSTRACT Despite the fact that around 200 cry genes from Bacillus thuringiensis have already been cloned, only a few Cry proteins are toxic towards a given pest. A crucial step in the mode of action of Cry proteins is binding to specific sites in the midgut of susceptible insects. Binding studies in insects that have developed cross-resistance discourage the combined use of Cry proteins sharing the same binding site. If resistance management strategies are to be implemented, the arsenal of Cry proteins suitable to control a given pest may be not so vast as it might seem at first. The present study evaluates the potential of B. thuringiensis for the control of a new pest, the geranium bronze…

endocrine systemBacterial ToxinsBacillus thuringiensisZoologymedicine.disease_causeApplied Microbiology and BiotechnologyBinding CompetitiveLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanymedicineInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalBinding SitesEcologybiologyBacillus thuringiensis ToxinsToxinGeranium bronzefungiLycaenidaeMidgutPlantsbiology.organism_classificationEndotoxinsLepidopteraPEST analysisFood ScienceBiotechnologyApplied and environmental microbiology
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Dissimilar Regulation of Antimicrobial Proteins in the Midgut of Spodoptera exigua Larvae Challenged with Bacillus thuringiensis Toxins or Baculoviru…

2015

Antimicrobial peptides (AMPs) and lysozymes are the main effectors of the insect immune system, and they are involved in both local and systemic responses. Among local responses, midgut immune reaction plays an important role in fighting pathogens that reach the insect body through the oral route, as do many microorganisms used in pest control. Under this point of view, understanding how insects defend themselves locally during the first phases of infections caused by food-borne pathogens is important to further improve microbial control strategies. In the present study, we analyzed the transcriptional response of AMPs and lysozymes in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae…

media_common.quotation_subjectAntimicrobial peptidesMolecular Sequence DataBacillus thuringiensislcsh:MedicineInsectSpodopteraSpodopteraMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaHemolymphAnimalsAmino Acid SequencePest Control Biologicallcsh:SciencePhylogenymedia_commonMultidisciplinarybiologyBacillus thuringiensis ToxinsSequence Homology Amino AcidMonophenol Monooxygenasefungilcsh:RMidgutbiology.organism_classificationEndotoxinsSettore AGR/11 - ENTOMOLOGIA GENERALE E APPLICATALarvaNoctuidaeInsect ProteinsMuramidaselcsh:QBaculoviridaeDigestive SystemAntimicrobial Cationic PeptidesResearch ArticlePLoS ONE
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Binding analysis of Bacillus thuringiensis Cry1 proteins in the sugarcane borer, Diatraea saccharalis (Lepidoptera: Crambidae).

2015

Sugarcane borer (Diatraea saccharalis, F.) is an important corn pest in South America and United States. The aim of the present study was to analyze the susceptibility and binding interactions of three Cry1A proteins and Cry1Fa in a Brazilian D. saccharalis population. The results showed that Cry1Ab was the most active, followed by Cry1Ac, Cry1Fa and Cry1Aa. All Cry1-biotinylated proteins tested bound specifically to the D. saccharalis brush border membrane vesicles (BBMV). Heterologous competition assays showed shared binding sites for all Cry1A proteins and another one shared by Cry1Fa and Cry1Ab. Thus, pyramiding Cry1Aa/Cry1Ac and Cry1F proteins would be a recommended strategy for managi…

media_common.quotation_subjectPopulationBacillus thuringiensisBiologyMothsDiatraea saccharalisCompetition (biology)Lepidoptera genitaliaInsecticide ResistanceHemolysin ProteinsCrambidaeBacterial ProteinsBacillus thuringiensisBotanyAnimalseducationPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commoneducation.field_of_studyBacillus thuringiensis Toxinsfungifood and beveragesbiology.organism_classificationEndotoxinsCry1AcPEST analysisJournal of invertebrate pathology
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