Search results for "Hemolysin"

showing 10 items of 169 documents

The Rapid Evolution of Resistance to Vip3Aa Insecticidal Protein in Mythimna separata (Walker) Is Not Related to Altered Binding to Midgut Receptors

2021

Laboratory selection for resistance of field populations is a well-known and useful tool to understand the potential of insect populations to evolve resistance to insecticides. It provides us with estimates of the frequency of resistance alleles and allows us to study the mechanisms by which insects developed resistance to shed light on the mode of action and optimize resistance management strategies. Here, a field population of Mythimna separata was subjected to laboratory selection with either Vip3Aa, Cry1Ab, or Cry1F insecticidal proteins from Bacillus thuringiensis. The population rapidly evolved resistance to Vip3Aa reaching, after eight generations, a level of >3061-fold resistance…

InsecticidesHealth Toxicology and Mutagenesismedia_common.quotation_subjectPopulationBacillus thuringiensisInsectMothsToxicologyInsecticide Resistance03 medical and health sciencesMythimna separataHemolysin ProteinsBacterial ProteinsBacillus thuringiensis<i>Bacillus thuringiensis</i>cross resistanceBt toxinsAnimalseducationCross-resistance030304 developmental biologymedia_commonGenetics0303 health sciencesLarvaeducation.field_of_studybiologyResistance (ecology)Bacillus thuringiensis Toxins030306 microbiologyCommunicationfungiRMidgutbiology.organism_classificationEndotoxinsLarvaoriental armywormMedicineProtein BindingToxins
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Tribolium castaneum Apolipophorin-III acts as an immune response protein against Bacillus thuringiensis Cry3Ba toxic activity

2013

In this study, a 2.1-fold Apolipophorin-III mRNA up-regulation was found in Tribolium castaneum larvae challenged with Bacillus thuringiensis Cry3Ba spore-crystal mixture. Knockdown of Apolipophorin-III by RNAi resulted in increased T. castaneum larvae susceptibility following Cry3Ba spore-crystal treatment, demonstrating Apolipophorin-III involvement in insect defense against B. thuringiensis. We showed that Apolipophorin-III participates in T. castaneum immune response to B. thuringiensis activating the prophenoloxidase cascade since: (i) phenoloxidase activity significantly increased after Cry3Ba spore-crystal treatment compared to untreated or Cry1Ac spore-crystal treated larvae and (ii…

Insecticidesanimal structuresBacillus thuringiensisBiologyMicrobiologyHemolysin ProteinsImmune systemBacterial ProteinsRNA interferenceImmunityBacillus thuringiensisToxicity TestsBotanyAnimalsEcology Evolution Behavior and SystematicsTriboliumGene knockdownBacillus thuringiensis ToxinsfungiProphenoloxidasebiology.organism_classificationImmunity InnateEndotoxinsApolipoproteinsCry1AcLarvaRNA InterferenceApolipophorin IIIJournal of Invertebrate Pathology
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Combining Hexanoic Acid Plant Priming with Bacillus thuringiensis Insecticidal Activity against Colorado Potato Beetle

2013

Interaction between insect herbivores and host plants can be modulated by endogenous and exogenous compounds present in the source of food and might be successfully exploited in Colorado potato beetle (CPB) pest management. Feeding tests with CPB larvae reared on three solanaceous plants (potato, eggplant and tomato) resulted in variable larval growth rates and differential susceptibility to Bacillus thuringiensis Cry3Aa toxin as a function of the host plant. An inverse correlation with toxicity was observed in Cry3Aa proteolytic patterns generated by CPB midgut brush-border membrane vesicles (BBMV) from Solanaceae-fed larvae, being the toxin most extensively proteolyzed on potato, followed…

Insecticidesmedicine.disease_causeMass Spectrometrylcsh:Chemistrychemistry.chemical_compoundHemolysin ProteinsPlant Growth RegulatorsCysteine ProteasesBacillus thuringiensisPlant defense against herbivoryColorado potato beetleElectrophoresis Gel Two-Dimensionallcsh:QH301-705.5SpectroscopySolanaceaeHexanoic acidbiologyfood and beveragesGeneral MedicineComputer Science ApplicationsColeopterasurgical procedures operativeBiochemistryLarvaHost-Pathogen Interactionsplant hormonesInsect ProteinsSolanaceaeproteolysisColoradoMolecular Sequence DataBacillus thuringiensisCatalysisArticleMicrobiologyCry3Aa toxinInorganic Chemistryintestain proteasesBacterial Proteinsplant defensemedicineAnimalsAmino Acid SequencePhysical and Theoretical ChemistryprimingMolecular BiologyCaproatesSolanum tuberosumBacillus thuringiensis ToxinsToxinOrganic ChemistryColorado potato beetlefungiBody WeightMidgutColorado potato beetle;<i> Bacillus thuringiensis</i>; Cry3Aa toxin; intestain proteases; proteolysis; Solanaceae; hexanoic acid; priming; plant defense; plant hormonesFeeding Behaviorbiology.organism_classificationDietEndotoxinsPapainchemistrylcsh:Biology (General)lcsh:QD1-999hexanoic acidPeptidesDigestive SystemSequence AlignmentInternational Journal of Molecular Sciences
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Broad-spectrum cross-resistance in Spodoptera exigua from selection with a marginally toxic Cry protein.

2009

BACKGROUND:Spodoptera exigua (Hubner) has developed resistance to a wide range of chemical insecticides. Products based on Bacillus thuringiensis Cry toxins are used in integrated pest management as an ecologically friendly alternative for pest control. Since there are few B. thuringiensis Cry proteins highly active against S. exigua, it is desirable to apply appropriate resistance management strategies to prevent the evolution of resistance to these proteins. RESULTS:Spodoptera exigua larvae were selected with Cry1Ab, a protein with low activity against this pest. Selected larvae developed > 30-fold resistance to Cry1Ab in 13 generations, relative to an unselected strain. The estimated rea…

Integrated pest managementInsecticidesBacillus thuringiensisSpodopteraSpodopteraToxicologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaAnimalsCross-resistancebiologyBacillus thuringiensis Toxinsbusiness.industryfungiPest controlGeneral Medicinebiology.organism_classificationBiotechnologyEndotoxinsInsect ScienceLarvaNoctuidaePEST analysisbusinessAgronomy and Crop SciencePest management science
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Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O.

2006

Following the observation that cells are able to recover from membrane lesions incurred by Staphylococcus aureus alpha-toxin and streptolysin O (SLO), we investigated the role of p38 in this process. p38 phosphorylation occurred in response to attack by both toxins, commencing within minutes after toxin treatment and waning after several hours. While SLO reportedly activates p38 via ASK1 and ROS, we show that this pathway does not play a major role for p38 induction in alpha-toxin-treated cells. Strikingly divergent effects of p38 blockade were noted depending on the toxin employed. In the case of alpha-toxin, inhibition of p38 within the time frame of its activation led to disruption of th…

KeratinocytesProgrammed cell deathStaphylococcus aureusCell Membrane Permeabilityp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologymedicine.disease_causeMAP Kinase Kinase Kinase 5Biochemistryp38 Mitogen-Activated Protein KinasesMicrobiologyHemolysin ProteinsAdenosine TriphosphateBacterial ProteinsProto-Oncogene ProteinsmedicineHumansASK1PhosphorylationMolecular BiologyCells CulturedPore-forming toxinToxinCell MembraneCell BiologyProtein-Tyrosine KinasesBlockadeCell biologyEnzyme ActivationStreptolysinsPhosphorylationStreptolysinBiochemical and biophysical research communications
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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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