Search results for "Hemolysin Protein"

showing 10 items of 156 documents

Staphylococcal alpha-toxin kills human keratinocytes by permeabilizing the plasma membrane for monovalent ions

1993

Incubation of human keratinocytes with nanomolar concentrations of Staphylococcus aureus alpha-toxin leads to irreversible depletion of cellular ATP. The toxin forms hexamers in the target cell membranes, and rapid transmembrane flux of K+, Na+, and 86Rb+ is observed. Unexpectedly, pores formed in keratinocytes through application of low but lethal doses of alpha-toxin appeared to be considerably smaller than those formed in erythrocyte membranes. They permitted neither rapid influx of Ca2+ or propidium iodide, nor efflux of carboxyfluorescein. Larger pores allowing flux of all three markers did form when the toxin was applied at high concentrations. Flux of monovalent ions and reduction in…

KeratinocytesStaphylococcus aureusCell Membrane PermeabilityBacterial ToxinsImmunologyMolecular ConformationBiologymedicine.disease_causeMicrobiologyCell membraneHemolysin Proteinschemistry.chemical_compoundOxygen ConsumptionNucleated cellmedicineExtracellularHumansPropidium iodideCells CulturedCell DeathToxinCell MembraneCations MonovalentCulture MediaMolecular WeightKineticsCytolysisInfectious Diseasesmedicine.anatomical_structureMembraneBiochemistrychemistryPotassiumBiophysicsCalciumParasitologyFlux (metabolism)Research ArticleInfection and Immunity
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Pore-forming Staphylococcus aureus alpha-toxin triggers epidermal growth factor receptor-dependent proliferation.

2006

Staphylococcal alpha-toxin is an archetypal killer protein that homo-oligomerizes in target cells to create small transmembrane pores. The membrane-perforating beta-barrel motif is a conserved attack element of cytolysins of Gram-positive and Gram-negative bacteria. Following the recognition that nucleated cells can survive membrane permeabilization, a profile of abundant transcripts was obtained in transiently perforated keratinocytes. Several immediate early genes were found to be upregulated, reminiscent of the cellular response to growth factors. Cell cycle analyses revealed doubling of S + G2/M phase cells 26 h post toxin treatment. Determination of cell counts uncovered that after an …

KeratinocytesStaphylococcus aureusSrc Homology 2 Domain-Containing Transforming Protein 1ImmunologyCellBacterial ToxinsBlotting WesternFluorescent Antibody TechniqueTransfectionMicrobiologyCell LineHemolysin ProteinsDownregulation and upregulationNucleated cellVirologymedicineHumansGrowth factor receptor inhibitorEpidermal growth factor receptorStaphylococcus aureus alpha toxinAdaptor Proteins Signal TransducingCell Line TransformedCell ProliferationbiologyCytotoxinsReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingCell CycleCell cycleFlow CytometryTransmembrane proteinCell biologyErbB Receptorsmedicine.anatomical_structureShc Signaling Adaptor Proteinsbiology.proteinMitogensSignal TransductionCellular microbiology
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Study of the bacillus thuringiensis Cry1Ia protein oligomerization promoted by midgut brush border membrane vesicles of lepidopteran and coleopteran …

2020

Bacillus thuringiensis (Bt) produces insecticidal proteins that are either secreted during the vegetative growth phase or accumulated in the crystal inclusions (Cry proteins) in the stationary phase. Cry1I proteins share the three domain (3D) structure typical of crystal proteins but are secreted to the media early in the stationary growth phase. In the generally accepted mode of action of 3D Cry proteins (sequential binding model), the formation of an oligomer (tetramer) has been described as a major step, necessary for pore formation and subsequent toxicity. To know if this could be extended to Cry1I proteins, the formation of Cry1Ia oligomers was studied by Western blot, after the incuba…

Leptinotarsa decemlineataBrush borderHealth Toxicology and MutagenesisBacillus thuringiensislcsh:MedicineSf21 cell lineOstrinia nubilalisToxicologyOligomer formationHemolysin Proteins<i>leptinotarsa decemlineata</i>03 medical and health sciencesWestern blotBacillus thuringiensisLobesia botranaSf9 CellsmedicineAnimalsProtein oligomerizationCry1AbIncubation<i>ostrinia nubilalis</i>030304 developmental biology0303 health sciencesBinding SitesBacillus thuringiensis ToxinsMicrovillimedicine.diagnostic_testbiology030306 microbiologyChemistryCommunicationVesiclelcsh:RfungiMembrane ProteinsMidgut<i>lobesia botrana</i>Trypsinbiology.organism_classificationColeopteraEndotoxinsLepidopteraBiochemistryBioassayProtein MultimerizationProtein Bindingmedicine.drug
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Staphylococcal alpha-toxin provokes neutrophil-dependent cardiac dysfunction: role of ICAM-1 and cys-leukotrienes.

2002

The role of polymorphonuclear neutrophils (PMN) in septic myocardial dysfunction is presently unknown. Staphylococcus aureus infections are frequently associated with septic sequelae. Therefore, we perfused isolated rat hearts with low doses of α-toxin, the major staphylococcal exotoxin, followed by application of human PMN, N-formyl-methionyl-leucyl-phenylalanine, and arachidonic acid. In contrast to sham-perfused hearts (no α-toxin), a rise in coronary perfusion pressure (CPP) and a reduction of contractile function were noted, and cardiac expression of intercellular adhesion molecule (ICAM)-1 was detected by immunohistochemical methods and real-time PCR. Histological analysis and myelope…

LeukotrienesHeart diseasePhysiologyNeutrophilsNeutrophileBacterial ToxinsExotoxinsThiophenesIn Vitro Techniquesmedicine.disease_causePathogenesisHemolysin ProteinsPhysiology (medical)medicineAnimalsHumansICAM-1Arachidonic AcidToxinbusiness.industryMyocardiumHydrazonesHeartmedicine.diseaseIntercellular Adhesion Molecule-1RatsN-Formylmethionine Leucyl-PhenylalaninePerfusionStaphylococcus aureusImmunologyCirculatory systemCardiology and Cardiovascular MedicinebusinessOligonucleotide ProbesExotoxinAmerican journal of physiology. Heart and circulatory physiology
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Effects of Escherichia coli hemolysin on human monocytes. Cytocidal action and stimulation of interleukin 1 release.

1990

Abstract This study reports on the potent cytocidal and interleukin-1 releasing properties of Escherichia coli hemolysin (ECH) on human monocytes. Nanomolar concentrations of purified ECH (250-2,000 ng/ml) caused rapid and irreversible depletion of cellular ATP to levels below 20% of controls within 60 min. Subcytocidal doses (10-200 ng/ml) of ECH induced rapid release within 60-120 min of large amounts of interleukin 1 beta (IL-1 beta) from cultured monocytes. IL-1 beta release occurred in the presence of actinomycin D and cycloheximide, and was thus probably due to processing and export of intracellular IL-1 beta precursor. Incubation of toxin-producing E. coli at ratios of only 0.3-3 col…

LipopolysaccharidesCell SurvivalStimulationIn Vitro TechniquesBiologyCycloheximidemedicine.disease_causeHemolysin ProteinsMonocytesMicrobiologyHemolysin Proteinschemistry.chemical_compoundAdenosine TriphosphateEscherichia colimedicineHumansEscherichia coliCells CulturedToxinMonokinesMonocyteInterleukinDrug SynergismGeneral Medicinemedicine.anatomical_structurechemistrySecretory RateIntracellularResearch ArticleInterleukin-1Journal of Clinical Investigation
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Stimulation of monokine production by lipoteichoic acids

1991

Lipoteichoic acids (LTAs) isolated from bacterial species, including Staphylococcus aureus, Streptococcus pyogenes A, Enterococcus faecalis, Streptococcus pneumoniae, and Listeria monocytogenes, were tested for their ability to stimulate the production of interleukin-1 beta (IL-1 beta), IL-6, and tumor necrosis factor alpha in cultured human monocytes. LTAs from S. aureus and S. pneumoniae failed to induce monokine production when applied in the concentration range of 0.05 to 5.0 micrograms/ml. However, LTAs from several enterococcal species (0.5 to 5 micrograms/ml) induced the release of all three monokines at levels similar to those observed after lipopolysaccharide stimulation. The kinet…

LipopolysaccharidesLipopolysaccharideAcylationBacterial ToxinsImmunologyBiologymedicine.disease_causeMicrobiologyEnterococcus faecalisMicrobiologyHemolysin ProteinsStructure-Activity Relationshipchemistry.chemical_compoundmedicineHumansInterleukin-6Tumor Necrosis Factor-alphaMonocyteDrug Synergismbiology.organism_classificationComplement systemTeichoic AcidsMonokineInfectious Diseasesmedicine.anatomical_structurechemistryStreptococcus pyogenesParasitologyTumor necrosis factor alphaLipoteichoic acidPeptidesInterleukin-1Research ArticleInfection and Immunity
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Identification of a putative membrane-inserted segment in the alpha-toxin of Staphylococcus aureus.

1994

To gain a fuller understanding of the regions of the Staphylococcus aureus alpha-toxin important in pore formation, we have used Forster dipole-dipole energy transfer to demonstrate that a central glycine-rich region of alpha-toxin (the so-called "hinge" region) inserts deeply into the bilayer on association of toxin with liposomes. Mutant alpha-toxins with unique cysteine (C) residues at positions 69 and 130 [Palmer, M., et al. (1993) J. Biol. Chem. 268, 11959) were reacted with the C-specific fluorophore acrylodan, which acted as an energy donor. The chosen acceptor was N-(7-nitrobenz-2-oxa-13- diazol-4-yl)-1,2-bis(hexadecanoyl)-sn-glycero-3-phosphoethanolamin e (NBD-PE). Measurement of t…

LiposomeStaphylococcus aureusQuenching (fluorescence)FluorophoreStereochemistryBilayerPhosphatidylethanolaminesBacterial ToxinsLipid BilayersMembrane ProteinsFluorescence PolarizationBiochemistryAcceptorLipidschemistry.chemical_compoundHemolysin ProteinsMembranechemistryMutagenesis Site-DirectedStaphylococcus aureus delta toxinCysteineFluorescent DyesBiochemistry
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Common, but Complex, Mode of Resistance of Plutella xylostella to Bacillus thuringiensis Toxins Cry1Ab and Cry1Ac

2005

ABSTRACT A field collected population of Plutella xylostella (SERD4) was selected in the laboratory with Bacillus thuringiensis endotoxins Cry1Ac (Cry1Ac-SEL) and Cry1Ab (Cry1Ab-SEL). Both subpopulations showed similar phenotypes: high resistance to the Cry1A toxins and little cross-resistance to Cry1Ca or Cry1D. A previous analysis of the Cry1Ac-SEL showed incompletely dominant resistance to Cry1Ac with more than one factor, at least one of which was sex influenced. In the present study reciprocal mass crosses between Cry1Ab-SEL and a laboratory susceptible population (ROTH) provided evidence that Cry1Ab resistance was also inherited as incompletely dominant trait with more than one factor…

MaleBacterial ToxinsPopulationBacillus thuringiensisMothsmedicine.disease_causeApplied Microbiology and BiotechnologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologymedicineAnimalsAllelePest Control BiologicaleducationGeneAllelesCrosses GeneticGenes DominantGeneticseducation.field_of_studyBacillus thuringiensis ToxinsEcologybiologyToxinbusiness.industryGenetic Complementation Testfungifood and beveragesPlutellabiology.organism_classificationBiotechnologyEndotoxinsCry1AcSusceptible individualBiological AssayFemalebusinessDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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Evaluating resistance to Bt Toxin Cry1Ab by F-2 Screen in European populations of Ostrinia nubilalis (Lepidoptera: Crambidae)

2010

The large-scale cultivation of transgenic crops producing Bacillus thuringiensis (Bt) toxins have already lead to the evolution of Bt resistance in some pest populations targeted by these crops. We used the F2 screening method for further estimating the frequency of resistance alleles of the European corn borer, Ostrinia nubilalis (Hübner) (Lepidoptera: Crambidae), to Bt maize, Zea mays L., producing the Cry1Ab toxin. In France, Germany, and Italy, 784, 455, and 80 lines of European corn borer were screened for resistance to Mon810 maize, respectively. In Slovakia, 26 lines were screened for resistance to the Cry1Ab toxin. The cost of F2 screen performed in the four countries varied from U.…

MaleBt maizeresistance management[SDV]Life Sciences [q-bio]Drug ResistanceZea maysHemolysin ProteinsBacterial ProteinsGermanyAnimalsEuropean corn borer Bt maize Mon810 resistance management HDR strategyPest Control BiologicalBacillus thuringiensis ToxinsReproductionfungifood and beveragesHDR strategyEndotoxinsEuropeLepidopteraeuropean corn borerSettore AGR/11 - Entomologia Generale E ApplicataCosts and Cost AnalysisFemaleFranceMon810
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ABCC transporters mediate insect resistance to multiple Bt toxins revealed by bulk segregant analysis

2014

[EN] Background: Relatively recent evidence indicates that ABCC2 transporters play a main role in the mode of action of Bacillus thuringiensis (Bt) Cry1A-type proteins. Mapping of major Cry1A resistance genes has linked resistance to the ABCC2 locus in Heliothis virescens, Plutella xylostella, Trichoplusia ni and Bombyx mori, and mutations in this gene have been found in three of these Bt-resistant strains. Results: We have used a colony of Spodoptera exigua (Xen-R) highly resistant to a Bt commercial bioinsecticide to identify regions in the S. exigua genome containing loci for major resistance genes by using bulk segregant analysis (BSA). Results reveal a region containing three genes fro…

MalePhysiologyGenes InsectPlant ScienceBt resistanceInsecticide ResistanceHemolysin ProteinsStructural BiologyBacillus thuringiensisChromosome SegregationPhylogenyGeneticsbiologyAgricultural and Biological Sciences(all)LarvaFemaleGeneral Agricultural and Biological SciencesBiotechnologyResearch ArticleMolecular Sequence DataBacillus thuringiensisSpodopteraSpodopteraABCC2 transporterPolymorphism Single NucleotideGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsExiguaAnimalsAmino Acid SequenceGeneEcology Evolution Behavior and SystematicsCrosses GeneticBombyxBacillus thuringiensis ToxinsBiochemistry Genetics and Molecular Biology(all)Gene Expression ProfilingfungiWild typeCell BiologySequence Analysis DNAbiology.organism_classificationBombyxMolecular biologyEndotoxinsKineticsGENETICACry1AcMembrane proteinATP-Binding Cassette TransportersCry toxinsDevelopmental Biology
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