Search results for "toxins"

showing 10 items of 799 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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Importance of Propionibacterium acnes hemolytic activity in human intervertebral discs: A microbiological study

2018

Most patients with chronic lower back pain (CLBP) exhibit degenerative disc disease. Disc specimens obtained during initial therapeutic discectomies are often infected/colonized with Propionibacterium acnes, a Gram-positive commensal of the human skin. Although pain associated with infection is typically ascribed to the body's inflammatory response, the Gram-positive bacterium Staphylococcus aureus was recently observed to directly activate nociceptors by secreting pore-forming α-hemolysins that disrupt neuronal cell membranes. The hemolytic activity of P. acnes in cultured disc specimens obtained during routine therapeutic discectomies was assessed through incubation on sheep-blood agar. T…

Bacterial DiseasesSensory ReceptorsPhysiologyStaphylococcusCellSocial SciencesHuman skinmedicine.disease_causePathology and Laboratory MedicineToxicologyMass SpectrometryAnalytical ChemistryPathogenesis0302 clinical medicineSpectrum Analysis TechniquesINFECTIONMedicine and Health SciencesNERVEAgarToxinsPsychologyStaphylococcus AureusIntervertebral DiscPOPULATIONMammals030222 orthopedicsMultidisciplinarybiologyQSTAPHYLOCOCCUSREukaryotaNociceptorsASSOCIATIONMatrix-Assisted Laser Desorption Ionization Mass SpectrometryRuminantsPREVALENCE3. Good healthBody FluidsBacterial PathogensChemistrymedicine.anatomical_structureBloodInfectious DiseasesStaphylococcus aureusMedical MicrobiologyPhysical SciencesVertebratesMedicineSensory PerceptionAnatomyPathogensLOW-BACK-PAINResearch ArticleSignal Transductionfood.ingredientScienceLower Back PainToxic AgentsPainResearch and Analysis MethodsMicrobiologyHemolysisDegenerative disc diseaseMicrobiology03 medical and health sciencesPropionibacterium acnesfoodSigns and SymptomsDiagnostic MedicinemedicineAnimalsHumansPropionibacterium acnesMicrobial PathogensStaphylococcal InfectionGram-Positive Bacterial InfectionsINNERVATIONSheepBacteriabusiness.industryOrganismsBiology and Life SciencesCell Biologymedicine.diseasebiology.organism_classificationAmniotesChronic DiseasebusinessLow Back Pain030217 neurology & neurosurgeryBacteriaNeurosciencePLoS ONE
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Integrative Model for Binding of Bacillus thuringiensis Toxins in Susceptible and Resistant Larvae of the Diamondback Moth (Plutella xylostella)

1999

ABSTRACT Insecticidal crystal proteins from Bacillus thuringiensis in sprays and transgenic crops are extremely useful for environmentally sound pest management, but their long-term efficacy is threatened by evolution of resistance by target pests. The diamondback moth ( Plutella xylostella ) is the first insect to evolve resistance to B. thuringiensis in open-field populations. The only known mechanism of resistance to B. thuringiensis in the diamondback moth is reduced binding of toxin to midgut binding sites. In the present work we analyzed competitive binding of B. thuringiensis toxins Cry1Aa, Cry1Ab, Cry1Ac, and Cry1F to brush border membrane vesicles from larval midguts in a susceptib…

Bacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsApplied Microbiology and BiotechnologyBinding CompetitiveModels BiologicalHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalGeneticsBacillaceaeDiamondback mothBinding SitesEcologybiologyBacillus thuringiensis ToxinsParasporal bodyfungiPlutellafood and beveragesbiology.organism_classificationEndotoxinsCry1AcLarvaFood ScienceBiotechnology
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Production and characterization of Bacillus thuringiensis Cry1Ac-resistant cotton bollworm Helicoverpa zea (Boddie).

2007

ABSTRACT Laboratory-selected Bacillus thuringiensis -resistant colonies are important tools for elucidating B. thuringiensis resistance mechanisms. However, cotton bollworm, Helicoverpa zea , a target pest of transgenic corn and cotton expressing B. thuringiensis Cry1Ac (Bt corn and cotton), has proven difficult to select for stable resistance. Two populations of H. zea (AR and MR), resistant to the B. thuringiensis protein found in all commercial Bt cotton varieties (Cry1Ac), were established by selection with Cry1Ac activated toxin (AR) or MVP II (MR). Cry1Ac toxin reflects the form ingested by H. zea when feeding on Bt cotton, whereas MVP II is a Cry1Ac formulation used for resistance se…

Bacterial ToxinsBacillus thuringiensisMothsGossypiumApplied Microbiology and BiotechnologyCypermethrinInsecticide Resistancechemistry.chemical_compoundHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsPest Control BiologicalGossypiumGenetically modified maizeEcologybiologyBacillus thuringiensis Toxinsfungifood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticulturechemistryAgronomyCry1AcBt cottonHelicoverpa zeaPEST analysisFood ScienceBiotechnologyProtein BindingApplied and environmental microbiology
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Comparison of Different Methodologies for Binding Assays of Bacillus thuringiensis Toxins to Membrane Vesicles from Insect Midguts

2002

Bacterial ToxinsBacillus thuringiensisMothsSpodopteraHemolysin ProteinsCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanymedicineAnimalsEcology Evolution Behavior and SystematicsBacillaceaeBacillus thuringiensis ToxinsbiologyVesicleCell MembraneMidgutbiology.organism_classificationBacillalesEndotoxinsmedicine.anatomical_structureBiochemistryDigestive SystemBacteriaJournal of Invertebrate Pathology
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Occurrence of a common binding site in Mamestra brassicae, Phthorimaea operculella, and Spodoptera exigua for the insecticidal crystal proteins CryIA…

1997

Specific binding to midgut membrane proteins is required for the toxicity of insecticidal crystal proteins (ICP) from Bacillus thuringiensis. A direct relationship between toxicity and binding has been proposed. It has been hypothesized that sharing of a single receptor by more than one ICP could lead to the occurrence of multiple resistance in the event of an alteration in the common receptor. Binding of CryIA(a), CryIA(b) and CryIA(c), three structurally related ICPs, has been studied in Phthorimaea operculella, Mamestra brassicae and, Spodoptera exigua using brush border membrane vesicles (BBMV) from the midgut tissue. Using iodinated CryIA(b), the three insects showed similar results: o…

Bacterial ToxinsBacillus thuringiensisReceptors Cell SurfaceSpodopteraMothsSpodopteraBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyAnimalsBinding siteReceptorMolecular BiologyBinding SitesbiologyBacillus thuringiensis ToxinsfungiMidgutbiology.organism_classificationMolecular biologyPhthorimaea operculellaEndotoxinsMembrane proteinInsect ScienceInsect ProteinsInsect biochemistry and molecular biology
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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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A comparative biochemical, pharmacological and immunological study of Clostridium novyi alpha-toxin, C. difficile toxin B and C. sordellii lethal tox…

1991

The three clostridial cytotoxins, i.e. alpha-toxin of C. novyi (Tox alpha-nov), toxin B of C. difficile (ToxB-dif) and lethal toxin of C. sordellii (LT-sor) consist of single peptide chains of about 200,000 (Tox alpha-nov), 250,000 (LT-sor) and 275,000 (ToxB-dif) mol. wts. ToxB-dif and LT-sor but not Tox alpha-nov cross-reacted with rabbit polyclonal antibodies. Toxicity upon i.v. injection in mice was similar (LD50, 100 hr, 50-200 ng/kg) and was characterized by a slowly developing fluid loss into the interstitial space. When injected into the rat paw the toxins caused a delayed local edema lasting for days. In vitro the three toxins provoked a persistent retraction of endothelial cells cu…

Bacterial ToxinsClostridium sordelliiClostridium difficile toxin BChick EmbryoBiologyPulmonary ArteryToxicologymedicine.disease_causeMedian lethal doseMicrobiologyLethal Dose 50chemistry.chemical_compoundMiceBacterial ProteinsmedicineAnimalsMicroscopy Phase-ContrastUridineCells CulturedClostridiumAdenosine Diphosphate RiboseToxinClostridioides difficileCytotoxinsRats Inbred Strainsbiology.organism_classificationClostridium novyiUridineRatsEndothelial stem cellchemistryADP-ribosylationPotassiumFemaleEndothelium VascularToxicon : official journal of the International Society on Toxinology
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