Search results for "Bacterial Toxins"

showing 10 items of 192 documents

Isolation and toxicity of Bacillus thuringiensis from potato-growing areas in Bolivia

2004

Bacillus thuringiensis was isolated from 116 samples collected in high altitude potato-growing areas in Bolivia. In these regions, main potato pests are the potato tuberworm Phthorimaea operculella, and the Andean weevils Premnotrypes latithorax and Rhigopsidius tucumanus. B. thuringiensis was found in 60% of the samples. The main percentage of samples with B. thuringiensis was found in larvae of R. tucumanus (78%). Bioassays were performed with 112 isolates. None resulted toxic to either larvae or adults of the two Andean weevils. However, 18 isolates from this study showed more toxicity against the beet armyworm Spodoptera exigua than the standard strain var. kurstaki isolated from DELFIN…

BoliviaVeterinary medicineBacterial ToxinsBacillus thuringiensisPolymerase Chain ReactionBacterial ProteinsBeet armywormBacillus thuringiensisExiguaBotanyAnimalsSoil MicrobiologyEcology Evolution Behavior and SystematicsSolanum tuberosumbiologyfungiDustbiology.organism_classificationGelechiidaePhthorimaea operculellaLepidopteraBiopesticideLarvaWeevilsElectrophoresis Polyacrylamide GelRestriction fragment length polymorphismPolymorphism Restriction Fragment LengthSolanaceaeJournal of Invertebrate Pathology
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Immunohistochemical Detection of Binding of Cryia Crystal Proteins of Bacillus thuringiensis in Highly Resistant Strains of Plutella xylostella (L.) …

1995

We detected binding of insecticidal crystal proteins from Bacillus thuringiensis in one susceptible strain and six resistant strains of diamondback moth, Plutella xylostella, from Hawaii. Immunohistochemical tests with tissue sections from larval midguts showed specific binding of CryIA(a), CryIA(b), and CryIA(c) to brush border membranes. CryIE, which is not toxic to P. xylostella, did not bind to midgut tissues. Larvae from one of the resistant strains ingested extremely high concentrations of a commercial formulation containing the three CryIA proteins without suffering midgut cell damage or mortality. This same resistant strain had previously been found to have greatly reduced binding o…

Brush borderBacterial ToxinsBacillus thuringiensisBiophysicsMothsHemolysin ProteinsBiochemistryEpitheliumHawaiiInsecticide ResistanceHemolysin ProteinsBacterial ProteinsIn vivoBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyDiamondback mothBacillus thuringiensis ToxinsMicrovillibiologyStrain (chemistry)fungiPlutellaMidgutCell Biologybiology.organism_classificationImmunohistochemistryMolecular biologyEndotoxinsLarvaBiochemical and Biophysical Research Communications
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Selective inhibition of binding of Bacillus thuringiensis Cry1Ab toxin to cadherin-like and aminopeptidase proteins in brush-border membranes and dis…

2007

Binding analyses with denatured epithelial membrane proteins from Bt (Bacillus thuringiensis) demonstrated at least two kinds of proteins, APNs (aminopeptidases N) and cadherin-like proteins, as possible receptors for the Cry1A class of Bt toxins. Two alternative models have been proposed, both based on initial toxin binding to a cadherin-like protein, but one involving APN and the other not. We have used two Bombyx mori strains (J65 and Kin), which are highly susceptible to Cry1Ab, to study the role of these two types of receptors on Cry1Ab toxin binding and cytotoxicity by means of the inhibitory effect of antibodies. BBMVs (brush-border membrane vesicles) of strain J65 incubated with lab…

Brush borderBacterial ToxinsBacillus thuringiensisCD13 Antigensmedicine.disease_causeBiochemistryAminopeptidaseAminopeptidasesAntibodiesHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsIntestinal MucosaReceptorMolecular BiologyMembranesbiologyBacillus thuringiensis ToxinsMicrovilliCadherinToxinfungiEpithelial CellsCell Biologybiology.organism_classificationBombyxMolecular biologyEndotoxinsMembrane proteinBiochemistrybiology.proteinBiological AssayAntibodyProtein BindingThe Biochemical journal
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Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)

2003

Abstract Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1…

Brush borderBacterial ToxinsBacillus thuringiensisGenetically modified cropsBinding CompetitiveBiochemistryMicrobiologyIodine RadioisotopesRadioligand AssayBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyBinding SitesMicrovillibiologyHeliothis virescensCytoplasmic Vesiclesfungifood and beveragesPlutellabiology.organism_classificationRecombinant ProteinsLepidopteraKineticsBt cottonCry1AcLarvaInsect ScienceProtein BindingPink bollwormInsect Biochemistry and Molecular Biology
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Bacillus thuringiensis crystal proteins CRY1Ab and CRY1Fa share a high affinity binding site in Plutella xylostella (L.).

1996

The future success of Bacillus thuringiensis based insecticides depends in part on our ability to prevent insects from developing resistance against their insecticidal crystal proteins. Two recent papers indicated cross-resistance between Cry1A proteins and Cry1Fa in two different insect species (Tabashnik et al., 1994, Appl. Environ. Microbiol. 60, 4627-4629; Gould et al., 1995, J. Econ. Entomol. 88, 1545-1559). Brush border membrane vesicles were prepared from Plutella xylostella and used in binding assays with 125I-labeled trypsin-activated crystal proteins. Competition experiments showed that Cry1Fa competed with Cry1Ab for a same binding site, though the latter still bound to a differe…

Brush borderBacterial ToxinsBiophysicsBacillus thuringiensisMothsHemolysin ProteinsBiochemistryCell membraneIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding siteReceptorPest Control BiologicalMolecular BiologyBinding SitesbiologyBacillus thuringiensis ToxinsVesiclefungiCell MembranePlutellaCell Biologybiology.organism_classificationMolecular biologyEndotoxinsmedicine.anatomical_structureBiochemistryBiochemical and biophysical research communications
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Development and Characterization of Diamondback Moth Resistance to Transgenic Broccoli Expressing High Levels of Cry1C

2000

ABSTRACT A field-collected colony of the diamondback moth, Plutella xylostella , had 31-fold resistance to Cry1C protoxin of Bacillus thuringiensis . After 24 generations of selection with Cry1C protoxin and transgenic broccoli expressing a Cry1C protein, the resistance that developed was high enough that neonates of the resistant strain could complete their entire life cycle on transgenic broccoli expressing high levels of Cry1C. After 26 generations of selection, the resistance ratios of this strain to Cry1C protoxin were 12,400- and 63,100-fold, respectively, for the neonates and second instars by a leaf dip assay. The resistance remained stable until generation 38 (G38) under continuous…

Brush borderBacterial ToxinsBrassicaGenetically modified cropsBrassicaMothsApplied Microbiology and BiotechnologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalDiamondback mothEcologybiologyStrain (chemistry)Bacillus thuringiensis ToxinsMicrovilliParasporal bodyfungibiology.organism_classificationPlants Genetically ModifiedMolecular biologyEndotoxinsFood ScienceBiotechnology
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Fighting mycobacterial infections by antibiotics, phytochemicals and vaccines.

2011

Buruli ulcer is a neglected disease caused by Mycobacterium ulcerans and represents the world's third most common mycobacterial infection. It produces the polyketide toxins, mycolactones A, B, C and D, which induce apoptosis and necrosis. Clinical symptoms are subcutaneous nodules, papules, plaques and ulcerating oedemae, which can enlarge and destroy nerves and blood vessels and even invade bones by lymphatic or haematogenous spread (osteomyelitis). Patients usually do not suffer from pain or systematic inflammation. Surgery is the treatment of choice, although recurrence is common and wide surgical excisions including healthy tissues result in significant morbidity. Antibiotic therapy wit…

Buruli ulcerNecrosismedicine.drug_classImmunologyAntibioticsBacterial ToxinsInflammationApoptosisQuinolonesMicrobiologyNecrosisBacterial ProteinsmedicineVaccines DNAAnimalsHumansBuruli UlcerbiologyMycobacterium ulceransbusiness.industryOsteomyelitisVaccinationNeglected DiseasesChaperonin 60medicine.diseasebiology.organism_classificationRifamycinsAnti-Bacterial AgentsVaccinationInfectious DiseasesLymphatic systemAminoglycosidesMycobacterium ulceransImmunologyBacterial VaccinesMacrolidesmedicine.symptombusinessPhytotherapyMicrobes and infection
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Pore-forming bacterial cytolysins

1998

Cell DeathCytotoxinsChemistryBacterial ToxinsCell MembraneAnimalsHumansGeneral MedicineIn Vitro TechniquesCrystallography X-RayApplied Microbiology and BiotechnologyBiotechnologyJournal of Applied Microbiology
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Autocatalytic cleavage of Clostridium difficile toxin B.

2007

Clostridium difficile, the causative agent of nosocomial antibiotic-associated diarrhoea and pseudomembranous colitis, possesses two main virulence factors: the large clostridial cytotoxins A and B. It has been proposed that toxin B is cleaved by a cytosolic factor of the eukaryotic target cell during its cellular uptake. Here we report that cleavage of not only toxin B, but also all other large clostridial cytotoxins, is an autocatalytic process dependent on host cytosolic inositolphosphate cofactors. A covalent inhibitor of aspartate proteases, 1,2-epoxy-3-(p-nitrophenoxy)propane, completely blocked toxin B function on cultured cells and was used to identify its catalytically active prote…

Cell ExtractsProteasesPhytic AcidSwineVirulence Factorsmedicine.medical_treatmentBacterial ToxinsClostridium difficile toxin AVirulenceClostridium difficile toxin Bmedicine.disease_causeCatalysisMicrobiologyCell LineNitrophenolsBiological FactorsBacterial ProteinsmedicineAnimalsAspartic Acid EndopeptidasesMultidisciplinaryProteaseBinding SitesToxinChemistryClostridioides difficilePseudomembranous colitisClostridium difficileProtein TransportBiochemistryEpoxy CompoundsProtein Processing Post-TranslationalSpleenNature
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Staphylococcal alpha-toxin: repair of a calcium-impermeable pore in the target cell membrane

2000

Staphylococcal alpha-toxin forms heptameric pores that render membranes permeable for monovalent cations. The pore is formed by an amphipathic beta-barrel encompassing amino acid residues 118-140 of each subunit of the oligomer. Human fibroblasts are susceptible to alpha-toxin but are able to repair the membrane lesions. Thereby, toxin oligomers remain embedded in the plasma membrane and exposed to the extracellular medium. In this study, we sought to detect structural changes occurring in the pore-forming sequence during lesion repair. Single cysteine substitution mutants were labelled with the environmentally sensitive fluorochrome acrylodan and, after mixing with wild-type toxin, incorpo…

Cell Membrane PermeabilityCalmodulinStaphylococcusBacterial ToxinsMicrobiologyCell membraneHemolysin Proteinschemistry.chemical_compoundmedicineExtracellularHumansLymphocytesLipid bilayerMolecular BiologyCells CulturedCytochalasin DbiologyCell MembraneLipid metabolismFibroblastsSpectrometry Fluorescencemedicine.anatomical_structureMembraneBiochemistrychemistrybiology.proteinBiophysicsCalciumCysteineMolecular Microbiology
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