Search results for "toxins"

showing 10 items of 799 documents

Botulinum A and the light chain of tetanus toxins inhibit distinct stages of Mg.ATP-dependent catecholamine exocytosis from permeabilised chromaffin …

1994

Susceptibilities of Mg.ATP-independent and Mg.ATP-requiring components of catecholamine secretion from digitonin-permeabilised chromaffin cells to inhibition by Clostridial botulinum type A and tetanus toxins were investigated. These toxins are Zn(2+)-dependent proteases which specifically cleave the 25-kDa synaptosomal-associated protein (SNAP-25) and vesicle-associated membrane protein (VAMP) II, respectively. When applied to permeabilised chromaffin cells they rapidly inhibited secretion in the presence of Mg.ATP but the catecholamine released in the absence of Mg.ATP, thought to represent fusion of primed granules, was not perturbed. The toxins can exert their effects per se in the abse…

ProteasesBotulinum ToxinsCell Membrane PermeabilityBiologymedicine.disease_causeBiochemistryExocytosisExocytosischemistry.chemical_compoundAdenosine TriphosphateCatecholaminesTetanus ToxinmedicineAnimalsSecretionChromaffin GranulesCells CulturedToxinKineticsmedicine.anatomical_structurechemistryMembrane proteinBiochemistryAdrenal MedullaCatecholamineCattleAdrenal medullaAdenosine triphosphatemedicine.drugEuropean journal of biochemistry
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Processing of tetanus and botulinum A neurotoxins in isolated chromaffin cells.

1995

Tetanus and botulinum A neurotoxins were introduced into the cytosol of chromaffin cells by means of an electric field in which the plasma membrane is forced to form pores of approximately 1 micron at the sites facing the electrodes. As demonstrated by electron microscopy, both [125I] and gold-labelled tetanus toxin (TeTx) diffuse through these transient openings. Dichain-TeTx, with its light chain linked to the heavy chain by means of a disulfide bond, causes the block of exocytosis to develop more slowly than does the purified light chain. The disulfide bonds, which in both toxins hold the subunits together, were cleaved by the intrinsic thioredoxin-reductase system. Single chain TeTx, in…

ProteasesBotulinum ToxinsCell Membrane PermeabilityProteolysisImmunoglobulin light chainmedicine.disease_causeExocytosisExocytosisTetanus ToxinmedicinePeptide bondAnimalsCells CulturedPharmacologymedicine.diagnostic_testToxinChemistryGeneral MedicineCytosolMicroscopy ElectronElectroporationBiochemistryAdrenal MedullaBiophysicsMicroscopy Electron ScanningCattleIntracellularNaunyn-Schmiedeberg's archives of pharmacology
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Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (…

2004

AbstractBinding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis δ-endotoxins.In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry…

ProteasesBrush borderBacterial ToxinsBacillus thuringiensisBiophysicsmedicine.disease_causeBinding CompetitiveBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsProtoxin activationBinding siteProtein PrecursorsChymotrypsinBinding SitesbiologyBacillus thuringiensis ToxinsMicrovilliToxinColorado potato beetleCell MembranefungiCell Biologybiology.organism_classificationTrypsinColeopteraEndotoxinsBiochemistryMode of actionbiology.proteinmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border memb…

2007

AbstractInsect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin–receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprote…

ProteasesCell Membrane PermeabilityPore formationProteolysismedicine.medical_treatmentBacterial ToxinsBacillus thuringiensisBiophysicsInsecticidal toxinBiochemistryCry3Aa proteolysisHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineColorado potato beetleAnimalsMetalloprotease inhibitorMetalloproteinaseBinding SitesProteaseBacillus thuringiensis ToxinsMicrovillibiologymedicine.diagnostic_testSecretory VesiclesAcetohydroxamic acidColorado potato beetleCell Biologybiology.organism_classificationProteaseColeopteraEndotoxinsModels ChemicalBiochemistryPorosityProtein Bindingmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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A cellular metalloproteinase activates Vibrio cholerae pro-cytolysin.

2004

Many strains of Vibrio cholerae produce a cytolysin (VCC) that forms oligomeric transmembrane pores in animal cells. The molecule is secreted as a procytolysin (pro-VCC) of 79 kDa that must be cleaved at the N terminus to generate the active 65-kDa toxin. Processing can occur in solution, and previous studies have described the action of mature VCC thus generated. However, little is known about the properties of pro-VCC itself. In this study, it is shown that pro-VCC exist as a monomer in solution and binds as a monomer to eukaryotic cells. Bound pro-VCC can then be activated either by exogenous, extracellular, or by endogenous, cell-bound proteases. In both cases, cleavage generates the 65…

ProteasesCholera Toxingenetic structuresCHO CellsBiologyADAM17 Proteinmedicine.disease_causeBiochemistryMiceCricetinaemedicineADAM17 ProteinAnimalsHumansProtein PrecursorsMolecular BiologyFurinMetalloproteinaseCytotoxinsCell MembraneMetalloendopeptidasesCell BiologyADAM Proteinseye diseasesTransmembrane proteinADAM ProteinsBiochemistryVibrio choleraebiology.proteinsense organsCytolysinRabbitsThe Journal of biological chemistry
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Functional significance of membrane associated proteolysis in the toxicity of Bacillus thuringiensis Cry3Aa toxin against Colorado potato beetle.

2012

Abstract Bacillus thuringiensis Cry toxins are widely used as biocontrol agents in bioinsecticides and transgenic plants. In the three domain-Cry toxins, domain II has been identified as an important determinant of their highly specific activity against insects. In this work, we assessed the role in membrane associated proteolysis and toxicity in Colorado potato beetle (CPB) of a previously reported ADAM recognition motif present in Cry3Aa toxin domain II. We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 344, 346, 347, 351 and 353 of the ADAM recognition motif in Cry3Aa toxin. Cry3Aa toxin mutants displayed decreased toxicity when comp…

ProteasesColoradoProteolysisMutantBacillus thuringiensisToxicologymedicine.disease_causeMicrobiologyHemolysin ProteinsRecognition sequenceBacterial ProteinsBacillus thuringiensismedicineAnimalsAmino Acid SequencePest Control BiologicalCells Culturedbiologymedicine.diagnostic_testBacillus thuringiensis ToxinsMicrovilliToxinfungiColorado potato beetleWild typeSequence Analysis DNAbiology.organism_classificationColeopteraEndotoxinsBiochemistryProteolysisMutagenesis Site-DirectedToxicon : official journal of the International Society on Toxinology
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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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Inhibition in vivo of the activity of botulinum neurotoxin A by small molecules selected by virtual screening

2012

To search for small molecular size inhibitors of botulinum neurotoxin A (BoNT/A) endopeptidase activity, we have screened the NCI library containing about 1 million structures against the substrate binding pocket of BoNT/A. Virtual screening (VS) was performed with the software Glide (Grid-based ligand docking energetics) and the findings were confirmed by AutoDock. Ten compounds were found that had favorable energetic and glide criteria and 5 of these compounds were selected for their ability to protect mice in vivo against a lethal dose of BoNT/A. Each compound was incubated at different molar excesses with a lethal dose of the toxin and then the mixture injected intravenously into mice. …

Protein ConformationToxinChemistryNeurotoxinsLethal doseComputational BiologyAutoDockPharmacologyProtective AgentsToxicologymedicine.disease_causeSmall moleculeToxicologyMiceEndopeptidase activityDocking (molecular)In vivoToxicitymedicineAnimalsBotulinum Toxins Type ASequence AlignmentSoftwareToxicon
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Expression and renaturation of the N-terminal extracellular domain of torpedo nicotinic acetylcholine receptor alpha-subunit.

1998

The N-terminal extracellular region (amino acids 1-209) of the alpha-subunit of the nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata electric tissue was expressed as inclusion bodies in Escherichia coli using the pET 3a vector. Employing a novel protocol of unfolding and refolding, in the absence of detergent, a water-soluble globular protein of 25 kDa was obtained displaying approximately 15% alpha-helical and 45% beta-structure. The fragment bound alpha-[3H]bungarotoxin in 1:1 stoichiometry with a KD value of 0.5 nM as determined from kinetic measurements (4 nM from equilibrium binding). The kinetics of association of toxin and fragment were of second order, with a similar …

Protein DenaturationProtein FoldingMolecular Sequence DataReceptors NicotinicTorpedoBiochemistrylaw.inventionchemistry.chemical_compoundGanglion type nicotinic receptorlawExtracellularmedicineEscherichia coliAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyMethyllycaconitineCell BiologyBungarotoxinBungarotoxinsRecombinant ProteinsNicotinic acetylcholine receptorBiochemistrychemistryAlpha-4 beta-2 nicotinic receptorTorpedoAcetylcholinemedicine.drugProtein BindingThe Journal of biological chemistry
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Acute cytotoxicity and apoptotic effects after l-Pam exposure in different cocultures of the proximal and distal respiratory system.

2009

Abstract Sulphur and nitrogen mustard are strong alkylating agents which can cause after inhalation acute lung injury in the larynx, trachea and large bronchi and can lead to alveolar edema. In our study we tested the N-Lost l -Phenylalanine Mustard ( l -Pam). Therefore we seeded the alveolar type II cell line NCI H441 on the upper membrane of a Transwell filter plate and the endothelial cell line ISO-Has-1 on the lower side of the membrane for the alveolar model and combined the human bronchial explant-outgrowth cells and fibroblasts in the bronchial model and exposed both models with various concentrations of l -Pam. Treatment with l -Pam led to a concentration-dependent decrease of the t…

ProteomeIntracellular SpaceBioengineeringApoptosisBronchiBiologyLung injuryApplied Microbiology and BiotechnologyCell Linechemistry.chemical_compoundMicroscopy Electron TransmissionmedicineElectric ImpedanceToxicity Tests AcuteHumansRespiratory systemMelphalanOrganellesAnalysis of VarianceLungCytotoxinsEndothelial CellsGeneral Medicinerespiratory systemMolecular biologyWI-38Nitrogen mustardCoculture TechniquesEndothelial stem cellPulmonary Alveolimedicine.anatomical_structurechemistryApoptosisImmunologyVacuolesIntracellularBiotechnologyJournal of biotechnology
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