Search results for "Hemolysin Protein"

showing 10 items of 156 documents

Simvastatin Inhibits Inflammatory Properties ofStaphylococcus aureusα-Toxin

2002

Background—Simvastatin, a 3-hydroxy-methylglutaryl coenzyme A reductase inhibitor, has been shown to lower serum cholesterol levels in clinical use. Moreover, statins exert beneficial effects in vascular diseases by inhibition of leukocyte rolling, adherence, and transmigration. The aim of this study was to determine if pretreatment with simvastatin attenuatesStaphylococcus aureusα-toxin–induced increase in leukocyte-endothelial interactions during exotoxemia.Methods and Results—The effects of simvastatin on leukocyte-endothelial cell interactions were observed by intravital microscopy in the rat mesenteric microcirculation. Simvastatin (50 or 100 μg/kg) was administered 18 hours before the…

MaleSimvastatinNitric Oxide Synthase Type IIIP-selectinEndotheliumBacterial ToxinsToxemiaInflammationLeukocyte RollingPharmacologyMicrocirculationRats Sprague-DawleyHemolysin ProteinsMesenteric VeinsVenulesCell MovementCulture TechniquesPhysiology (medical)Cell AdhesionLeukocytesmedicineAnimalsMicroscopy Videobusiness.industryAnti-Inflammatory Agents Non-SteroidalHemodynamicsStaphylococcal InfectionsImmunohistochemistryRatsEndothelial stem cellP-Selectinmedicine.anatomical_structureSimvastatinImmunologyEndothelium VascularHydroxymethylglutaryl-CoA Reductase InhibitorsNitric Oxide Synthasemedicine.symptomCardiology and Cardiovascular MedicinebusinessIntravital microscopymedicine.drugCirculation
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Regulation of phospholipase D activity in synaptosomes permeabilized with Staphylococcus aureus alpha-toxin.

1998

In order to investigate the regulation of presynaptic phospholipase D (PLD) activity by calcium and G proteins, we established a permeabilization procedure for rat cortical synaptosomes using Staphylococcus aureus alpha-toxin (30-100 microg/ml). In permeabilized synaptosomes, PLD activity was significantly stimulated when the concentration of free calcium was increased from 0.1 microM to 1 microM. This activation was inhibited in the presence of KN-62 (1 microM), an inhibitor of calcium/calmodulin-dependent kinase II (CaMKII), but not by the protein kinase C inhibitor, Ro 31-8220 (1-10 microM). Synaptosomal PLD activity was also stimulated in the presence of 1 microM GTPgammaS. When Rho pro…

MaleStaphylococcus aureusCell Membrane PermeabilityG proteinBacterial ToxinsBiophysicschemistry.chemical_elementCalciumBiologyIn Vitro TechniquesBiochemistryClostridium difficile toxin Bchemistry.chemical_compoundHemolysin ProteinsStructural BiologyStaphylococcus aureus α-toxinCa2+/calmodulin-dependent protein kinaseSynaptosomeGeneticsPhospholipase DPhospholipase D activityAnimalsRats WistarMolecular BiologyProtein kinase CSynaptosomePhospholipase DRho proteinCalcium/calmodulin-dependent protein kinase IICell BiologyBrefeldin AMolecular biologyRatsEnzyme Activationenzymes and coenzymes (carbohydrates)BiochemistrychemistryGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)CalciumSynaptosomesFEBS letters
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Staphylococcal α-toxin provokes coronary vasoconstriction and loss in myocardial contractility in perfused rat hearts: Role of thromboxane generation

2000

Background —Cardiac performance is severely depressed in septic shock. Endotoxin has been implicated as the causative agent in Gram-negative sepsis, but similar abnormalities are encountered in Gram-positive sepsis. We investigated the influence of the major exotoxin of Staphylococcus aureus, staphylococcal α-toxin, in isolated perfused rat hearts. Methods and Results —α-Toxin 0.25 to 1 μg/mL caused a dose-dependent increase in coronary perfusion pressure that more than doubled. In parallel, we noted a decrease in left ventricular developed pressure and the maximum rate of left ventricular pressure rise (dP/dt max ), dropping to a minimum of <60% of control. These changes were accompani…

MaleThromboxaneIndomethacinProstacyclinVentricular Function LeftHemolysin ProteinsThromboxane A2chemistry.chemical_compoundEdemaPhenylacetatesSulfonamidesHeartAzepinesPerfusionAnesthesiaLactatesVentricular pressuremedicine.symptomCardiology and Cardiovascular Medicinemedicine.drugStaphylococcus aureusmedicine.medical_specialtyBacterial ToxinsExotoxinsIn Vitro TechniquesSepsisContractilityThromboxane A2Physiology (medical)Internal medicinemedicineAnimalsMasoprocolPlatelet Activating FactorRats WistarAspirinL-Lactate Dehydrogenasebusiness.industryTriazolesmedicine.diseaseEpoprostenolMyocardial ContractionRatsEndocrinologychemistryVasoconstrictionPotassiumCoronary perfusion pressurebusinessPlatelet Aggregation InhibitorsVasoconstriction
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Characterization ofBacillus thuringiensisisolated from infections in burn wounds

1997

Four strains of Bacillus thuringiensis were isolated from infections in burn wounds and from water used in the treatment of burn wounds. The strains produced large parasporal inclusion bodies composed of 141, 83, and 81 kDa protoxins. The four strains were tested for insecticidal activity against larvae of Pieris brassicae and Aedes aegypti but showed no activity; Vero cell assays for the production of enterotoxins were also negative. Attempts to classify the strains according to flagellar H-serotype showed them all to be non-flagellated. Apart from two occupational health accidents that occurred during the handling of highly concentrated B. thuringiensis fluids, this is the first report of…

Microbiology (medical)Bacterial ToxinsImmunologyBacillus thuringiensisBacillus cereusAedes aegyptiEnterotoxinMicrobiologyMicrobiologyHemolysin ProteinsBacterial ProteinsAedesBacillus thuringiensisChlorocebus aethiopsAnimalsHumansImmunology and AllergyVero CellsPieris brassicaeBacillus thuringiensis Toxinsbiologybacillus thurigiensisinfectionsfungiGeneral Medicinebiology.organism_classificationBacillalesVirologyEndotoxinsInfectious DiseasesWound InfectionVero cellBurnsButterfliesBacteriaFEMS Immunology & Medical Microbiology
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In vivo effects of intravascularly applied Escherichia coli hemolysin: dissociation between induction of granulocytopenia and lethality in monkeys.

1993

The effects of intravascular application of endotoxin-depleted Escherichia coli hemolysin (HlyA) was studied in rabbits and monkeys. In rabbits, bolus application of HlyA calculated to effect final blood levels of approximately 2-3 HU/ml (200-300 ng/ml) caused an acute fall of polymorphonuclear blood leukocytes to less than 20% of starting levels within 5 min. Additionally, platelet counts dropped to approximately 30% of starting levels, whereas lymphocyte counts varied considerably and seldom fell to less than 50%. Nine out ten animals that received 2-4 HU/ml toxin died within 90 min post application. These animals presented with signs of acute respiratory failure and post mortem inspectio…

Microbiology (medical)Blood Plateletsmedicine.medical_specialtyPathologyLymphocyteImmunologyBacterial ToxinsSpleenBlood PressurePulmonary EdemaBiologyPulmonary sequestrationLethal Dose 50Hemolysin ProteinsBacterial ProteinsIn vivoInternal medicinemedicineEscherichia coliImmunology and AllergyAnimalsLungLeukopeniaLungDose-Response Relationship DrugPancreatic ElastaseEscherichia coli ProteinsElastaseGeneral Medicinemedicine.diseasePulmonary edemaBlood Cell CountCapillariesMacaca fascicularisEndocrinologymedicine.anatomical_structureInjections Intra-ArterialLiverInjections IntravenousRabbitsmedicine.symptomSpleenAgranulocytosisGranulocytesMedical microbiology and immunology
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Staphylococcus aureus α-Toxin’s Close Contacts Ensure the Kill

2018

The membrane pore-forming α-toxin is an important virulence factor of Staphylococcus aureus. Target cells can remove pores from their surface, but recent work shows that α-toxin may undermine this self-defense by clinging to epithelial cell junctions. The findings could lead to the development of novel remedies against S. aureus infections.

Microbiology (medical)Staphylococcus aureusVirulence FactorsBacterial ToxinsBiologymedicine.disease_causeMicrobiologyVirulence factorCell LineMicrobiologyAdherens junctionADAM10 ProteinHemolysin Proteins03 medical and health sciencesVirologymedicineAnimalsHumans030304 developmental biology0303 health sciencesPore-forming toxin030306 microbiologyMembrane ProteinsEpithelial CellsAdherens JunctionsStaphylococcal InfectionsEpitheliumInfectious Diseasesmedicine.anatomical_structureStaphylococcus aureusPinocytosisCarrier ProteinsTrends in Microbiology
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A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes

1993

Depending on the size of the pores one wishes to produce in plasma membranes, the choice will probably fall on one of the three toxins discussed above. S. aureus alpha-toxin should be tried first when pores of 1-1.5 nm diameter are required. This is generally the case when Ca2+ and nucleotide dependence of a given process is being studied. If alpha-toxin does not work, this is probably due to the fact that the toxin either does not produce pores, or that the pores are too small. In this case, high concentrations of alpha-toxin should be tried. If this still does not work, we recommend the use of HlyA. When very large pores are to be created, e.g. for introduction of antibodies into the cell…

Microbiology (medical)TetanolysinPore-forming toxinCell Membrane PermeabilityEscherichia coli ProteinsEscherichia coli ProteinsBacterial ToxinsCell MembraneImmunologyGeneral MedicineMembrane transportBiologyHemolysin Proteinschemistry.chemical_compoundMembraneBacterial ProteinschemistryBiochemistryStreptolysinsBiophysicsImmunology and AllergyCell permeabilityMedical Microbiology and Immunology
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Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
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Interaction of Heparins and Dextran Sulfates with a Mesoscopic Protein Nanopore

2009

A mechanism of how polyanions influence the channel formed by Staphylococcus aureus alpha-hemolysin is described. We demonstrate that the probability of several types of polyanions to block the ion channel depends on the presence of divalent cations and the polyanion molecular weight and concentration. For heparins, a 10-fold increase in molecular weight decreases the half-maximal inhibitory concentration, IC(50), nearly 10(4)-fold. Dextran sulfates were less effective at blocking the channel. The polyanions are significantly more effective at reducing the conductance when added to the trans side of this channel. Lastly, the effectiveness of heparins on the channel conductance correlated wi…

Models MolecularStereochemistryBacterial ToxinsLipid BilayersMolecular ConformationBiophysicsmacromolecular substancesDivalentIonchemistry.chemical_compoundHemolysin ProteinsCysteineChannels and TransportersLipid bilayerIon channelchemistry.chemical_classificationMesoscopic physicsHeparinCell MembraneElectric Conductivitytechnology industry and agricultureConductanceDextransNanostructuresNanoporeDextranchemistryLiposomesMutationBiophysicsPorosityProtein BindingBiophysical Journal
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Variability in the cadherin gene in an Ostrinia nubilalis strain selected for Cry1Ab resistance

2008

Transgenic corn expressing Cry1Ab (a Bacillus thuringiensis toxin) is highly effective in the control of Ostrinia nubilalis. For its toxic action, Cry1Ab has to bind to specific insect midgut proteins. To date, in three Lepidoptera species resistance to a Cry1A toxin has been conferred by mutations in cadherin, a protein of the Lepidoptera midgut membrane. The implication of cadherin in the resistance of an Ostrinia nubilalis colony (Europe-R) selected with Bacillus thuringiensis Cry1Ab protoxin was investigated. Several major mutations in the cadherin (cdh) gene were found, which introduced premature termination codons and/or large deletions (ranging from 1383 to 1701bp). The contribution …

MutantDrug ResistanceGenetically modified cropsMothsBiologyBiochemistryOstriniaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyGenetic variationAnimalsMolecular BiologyGeneGeneticsPolymorphism GeneticBacillus thuringiensis ToxinsCadherinfungiGenetic Variationfood and beveragesMidgutCadherinsbiology.organism_classificationEndotoxinsInsect ScienceMutationInsect ProteinsInsect Biochemistry and Molecular Biology
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