Search results for "Epido"

showing 10 items of 238 documents

Effect of Bacillus thuringiensis toxins on the midgut of the nun moth Lymantria monacha.

2000

Three steps of the proposed mode of action of Bacillus thuringiensis toxins have been studied in Lymantria monacha. We demonstrated that only the toxins that caused typical pathological changes in midgut epithelial cells and bound to the midgut brush border membrane were able to drastically reduce the midgut transepithelial voltage of the nun moth.

BacillaceaebiologyBrush borderfungiBacterial ToxinsBacillus thuringiensisMidgutMothsbiology.organism_classificationdigestive systemBacillalesMicrobiologyLepidoptera genitaliaIntestinesBacillus thuringiensisparasitic diseasesAnimalssense organsMode of actionEcology Evolution Behavior and SystematicsTransepithelial potential differenceJournal of invertebrate pathology
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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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Resistance to the Bacillus thuringiensis bioinsecticide in a field population of Plutella xylostella is due to a change in a midgut membrane receptor.

1991

The biochemical mechanism for resistance to Bacillus thuringiensis crystal proteins was studied in a field population of diamondback moths (Plutella xylostella) with a reduced susceptibility to the bioinsecticidal spray. The toxicity and binding characteristics of three crystal proteins [CryIA(b), CryIB, and CryIC] were compared between the field population and a laboratory strain. The field population proved resistant (greater than 200-fold compared with the laboratory strain) to CryIA(b), one of the crystal proteins in the insecticidal formulation. Binding studies showed that the two strains differ in a membrane receptor that recognizes CryIA(b). This crystal protein did not bind to the b…

Bacterial ToxinsBacillus thuringiensismedicine.disease_causeBinding CompetitiveMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineEscherichia coliAnimalsPest Control BiologicalEscherichia coliMultidisciplinaryBacillaceaebiologyStrain (chemistry)Bacillus thuringiensis ToxinsMicrovilliParasporal bodyPlutellaMidgutGene Expression Regulation Bacterialbiology.organism_classificationBacillalesMolecular biologyEndotoxinsLepidopteraGenes BacterialResearch Article
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Common receptor for Bacillus thuringiensis toxins Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea and Spodoptera exigua

2005

ABSTRACT Binding studies using 125 I-Cry1Ac and biotinylated Cry1Fa toxins indicate the occurrence of a common receptor for Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera , Helicoverpa zea , and Spodoptera exigua . Our results, along with previous binding data and the observed cases of cross-resistance, suggest that this pattern seems to be widespread among lepidopteran species.

Bacterial ToxinsBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaReceptors Cell SurfaceSpodopteraHelicoverpa armigeraSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyInvertebrate MicrobiologyAnimalsBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungibiology.organism_classificationEndotoxinsLepidopteraCry1AcInsect ProteinsNoctuidaeHelicoverpa zeaFood ScienceBiotechnology
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Shared Binding Sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A Toxins

2001

ABSTRACT Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth ( Plutella xylostella ) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that…

Bacterial ToxinsMolecular Sequence DataSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsAmino Acid SequenceBinding siteBinding SitesDiamondback mothBacillus thuringiensis ToxinsEcologybiologyHeliothis virescensfungibiology.organism_classificationEndotoxinsLepidopteraPlutellidaeCry1AcLarvaNoctuidaeFood ScienceBiotechnologyApplied and Environmental Microbiology
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Interaction of Bacillus thuringiensis Toxins with Larval Midgut Binding Sites of Helicoverpa armigera (Lepidoptera: Noctuidae)

2004

ABSTRACT In 1996, Bt-cotton (cotton expressing a Bacillus thuringiensis toxin gene) expressing the Cry1Ac protein was commercially introduced to control cotton pests. A threat to this first generation of transgenic cotton is the evolution of resistance by the insects. Second-generation Bt-cotton has been developed with either new B. thuringiensis genes or with a combination of cry genes. However, one requirement for the “stacked” gene strategy to work is that the stacked toxins bind to different binding sites. In the present study, the binding of 125 I-labeled Cry1Ab protein ( 125 I-Cry1Ab) and 125 I-Cry1Ac to brush border membrane vesicles (BBMV) of Helicoverpa armigera was analyzed in com…

Bacterial ToxinsPopulationBacillus thuringiensisCarbohydratesDrug ResistanceHelicoverpa armigeraModels BiologicalApplied Microbiology and BiotechnologyMicrobiologyHemolysin Proteinschemistry.chemical_compoundBacterial ProteinsLectinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsBinding siteSoybean agglutininPest Control BiologicaleducationGossypiumeducation.field_of_studyBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungifood and beveragesPlants Genetically Modifiedbiology.organism_classificationSialic acidEndotoxinsLepidopteraKineticsCry1AcchemistryBiochemistryGenes BacterialLarvaNoctuidaeDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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Microbial Diversity in the Midguts of Field and Lab-Reared Populations of the European Corn Borer Ostrinia nubilalis

2011

Background: Insects are associated with microorganisms that contribute to the digestion and processing of nutrients. The European Corn Borer (ECB) is a moth present world-wide, causing severe economical damage as a pest on corn and other crops. In the present work, we give a detailed view of the complexity of the microorganisms forming the ECB midgut microbiota with the objective of comparing the biodiversity of the midgut-associated microbiota and explore their potential as a source of genes and enzymes with biotechnological applications. Methodological/Principal Findings: A high-throughput sequencing approach has been used to identify bacterial species, genes and metabolic pathways, parti…

Bacterium identificationEuropean corn borerMicrobial diversityEuropean corn borerStaphylococcusBiodiversityOstrinia nubilalisNegibacteriaMothsAnimal tissueOstriniaMidgutMicrobial population dynamicsBacteria (microorganisms)PhylogenyMultidisciplinaryIntestine floraEcologybiologyBacterial geneSystems BiologyQRHexapodafood and beveragesAgricultureGenomicsLepidopteraPosibacteriaMAQUINAS Y MOTORES TERMICOSMedicineSynthetic BiologySequence AnalysisResearch ArticleBiotechnologyScienceBiological Data ManagementBacterial genomeMicrobiologydigestive systemZea maysArticleLepidoptera genitaliaMetabolic NetworksGeneticsAnimalsMicrobiomeBiologyWeissella paramesenteroidesBacteriabusiness.industryfungiStaphylococcus warneriComputational BiologyMidgutPopulation abundancebiology.organism_classificationNonhumanBiotechnologyAgronomyMetagenomicsWeissellaFISICA APLICADAMetagenomePEST analysisbusinessControlled studyAgroecology
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Specific binding  of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species

2008

ABSTRACT For a long time, it has been assumed that the mode of action of Cry2A toxins was unique and different from that of other three-domain Cry toxins due to their apparent nonspecific and unsaturable binding to an unlimited number of receptors. However, based on the homology of the tertiary structure among three-domain Cry toxins, similar modes of action for all of them are expected. To confirm this hypothesis, binding assays were carried out with 125 I-labeled Cry2Ab. Saturation assays showed that Cry2Ab binds in a specific and saturable manner to brush border membrane vesicles (BBMVs) of Helicoverpa armigera . Homologous-competition assays with 125 I-Cry2Ab demonstrated that this toxi…

BioquímicaBrush borderBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaPlasma protein bindingHelicoverpa armigeraApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteHelicoverpaBacillus thuringiensis ToxinsStaining and LabelingEcologybiologyfungiMidgutbiology.organism_classificationEndotoxinsGastrointestinal TractLepidopteraKineticsBiochemistryHelicoverpa zeaProteïnesProtein BindingFood ScienceBiotechnology
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Lack of Cry1Fa binding to the midgut brush border membrane in a resistant colony of Plutella xylostella moths with a mutaton in the ABCC2 locus

2012

ABSTRACT Previous studies reported “mode 1” Bacillus thuringiensis resistance in a colony of diamondback moths (NO-QA), and recently, this resistance has been mapped to an ABC transporter ( ABCC2 ) locus. We report the lack of binding of Cry1Fa to insects derived from this colony and compare our data with those from other insects with ABCC2 -associated resistance.

BioquímicaBrush borderBiotecnologia agrícolaDrug ResistanceResistència als plaguicidesLocus (genetics)ATP-binding cassette transporterDrug resistanceApplied Microbiology and BiotechnologyLepidoptera genitaliaHemolysin ProteinsPlagues ControlBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsGeneticsBacillus thuringiensis ToxinsMicrovilliEcologybiologyfungiPlutellaMidgutbiology.organism_classificationMultidrug Resistance-Associated Protein 2EndotoxinsLepidopteraMutationMultidrug Resistance-Associated ProteinsProtein BindingFood ScienceBiotechnology
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Specific binding of radiolabeled Cry1Fa insecticidal protein from Bacillus thuringiensis to midgut sites in lepidopteran species

2012

ABSTRACT Cry1Fa insecticidal protein was successfully radiolabeled with 125 I-Na. Specific binding to brush border membrane vesicles was shown for the lepidopteran species Ostrinia nubilalis , Spodoptera frugiperda , Spodoptera exigua , Helicoverpa armigera , Heliothis virescens , and Plutella xylostella . Homologous competition assays were performed to obtain equilibrium binding parameters ( K d [dissociation constant] and R t [concentration of binding sites]) for these six insect species.

BioquímicavirusesBiotecnologia agrícolaBacillus thuringiensisHelicoverpa armigeraSpodopteraSpodopteraApplied Microbiology and BiotechnologyOstriniaIodine RadioisotopesHemolysin ProteinsPlagues ControlBacterial ProteinsSpecies SpecificityBacillus thuringiensisExiguaBotanyparasitic diseasesPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteTransport VesiclesBinding SitesEcologybiologyHeliothis virescensBacillus thuringiensis ToxinsMicrovillifungiPlutellabiology.organism_classificationEndotoxinsLepidopteraBiochemistryDigestive SystemProteïnesFood ScienceBiotechnology
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