Search results for "Hemolysin Protein"

showing 10 items of 156 documents

Dissecting the role of ADAM10 as a mediator of Staphylococcus aureus α-toxin action

2016

Staphylococcus aureus is a leading cause of bacterial infections in humans, including life-threatening diseases such as pneumonia and sepsis. Its small membrane-pore-forming α-toxin is considered an important virulence factor. By destroying cell–cell contacts through cleavage of cadherins, the metalloproteinase ADAM10 (a disintegrin and metalloproteinase 10) critically contributes to α-toxin-dependent pathology of experimental S. aureus infections in mice. Moreover, ADAM10 was proposed to be a receptor for α-toxin. However, it is unclear whether the catalytic activity or specific domains of ADAM10 are involved in mediating binding and/or subsequent cytotoxicity of α-toxin. Also, it is not k…

0301 basic medicineStaphylococcus aureusADAM10Bacterial Toxinsmedicine.disease_causeBiochemistryVirulence factorADAM10 ProteinHemolysin ProteinsMice03 medical and health sciencesCatalytic DomainmedicineDisintegrinAnimalsMolecular BiologyFurinCells CulturedMice KnockoutMetalloproteinasebiologyCadherinCell MembraneCell BiologyStaphylococcal InfectionsCadherinsCell biology030104 developmental biologyBiochemistryStaphylococcus aureusbiology.proteinCalciumIntracellularProtein BindingBiochemical Journal
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The usefulness of a mathematical model of exposure for environmental risk assessment

2011

We respond to the Comment of Lang et al . [[1][1]] regarding our mathematical model [[2][2]] of exposure of non-target Lepidoptera to Bt -maize pollen expressing Cry1Ab within Europe. Lang et al . remark on the degree to which the model was subject to uncertainty. Perry et al . [[2][2]] did indeed

1001Insecticides60Bacillus thuringiensisBiologyMothsModels BiologicalRisk AssessmentZea maysGeneral Biochemistry Genetics and Molecular BiologyBacterial proteinHemolysin ProteinsBacterial ProteinsAnimalsPest Control BiologicalGeneral Environmental ScienceEnvironmental risk assessmentBt corn Cry IAb Lepidoptera31General Immunology and MicrobiologyBacillus thuringiensis ToxinsEcologyComments and Invited RepliesGeneral MedicinePlants Genetically ModifiedZea maysEndotoxinsEuropePollenGeneral Agricultural and Biological SciencesMathematical economicsButterfliesProceedings of the Royal Society B: Biological Sciences
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A mathematical model of exposure of nontarget Lepidoptera to Bt-maize pollen expressing Cry1Ab within Europe

2010

Genetically modified (GM) maize MON810 expresses a Cry1Ab insecticidal protein, derived from Bacillus thuringiensis ( Bt ), toxic to lepidopteran target pests such as Ostrinia nubilalis . An environmental risk to non-target Lepidoptera from this GM crop is exposure to harmful amounts of Bt -containing pollen deposited on host plants in or near MON810 fields. An 11-parameter mathematical model analysed exposure of larvae of three non-target species: the butterflies Inachis io (L.), Vanessa atalanta (L.) and moth Plutella xylostella (L.), in 11 representative maize cultivation regions in four European countries. A mortality–dose relationship was integrated with a dose–distance relationship t…

1001genetically modified maize Cry1Ab non-target Lepidoptera mathematical model exposure risk assessment60Bacillus thuringiensismedicine.disease_causeZea maysModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyOstriniaExposureCropLepidoptera genitaliaHemolysin ProteinsMathematical modelBacterial ProteinsResearch articlesPollenBacillus thuringiensismedicineAnimalsPest Control BiologicalGeneral Environmental ScienceRisk assessmentGenetically modified maize31General Immunology and MicrobiologybiologyBacillus thuringiensis Toxinsbusiness.industryfungiPest controlPlutellafood and beveragesGeneral MedicineNon-target lepidopterabiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraAgronomyGenetically modified maizePollenCry1abGeneral Agricultural and Biological SciencesbusinessButterflies
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The Vibrio choleare haemolysin anion channel is required for cell vacuolation and death

2002

SummarySeveral strains of Vibrio cholerae secrete ahaemolytic toxin of 63kDa, termed V. cholerae cytolysin (VCC). This toxin causes extensive vacuo-lation and death of cells in culture and forms ananion-selective channel in planar lipid bilayers and incells. Here, we identify inhibitors of the VCC anionchannel and show that the formation of the anionchannel is necessary for the development of the vacuoles and for the cell death induced by this toxin. Using markers of cell organelles, we show that vacuoles derive from different intracellular com-partments and we identify the contribution of lateendosomes and of the trans -Golgi network in vacuolebiogenesis.Introduction The Gram-negative bact…

4-Acetamido-4'-isothiocyanatostilbene-22'-disulfonic AcidImmunologyLipid BilayersVirulenceGolgi ApparatusVacuoleEndosomesBiology44'-Diisothiocyanostilbene-22'-Disulfonic AcidIn Vitro Techniquesmedicine.disease_causeTransfectionMicrobiologyModels BiologicalAmmonium ChlorideIon ChannelsMicrobiologyCell LineHemolysin ProteinsBacterial ProteinsVirologyOrganelleChlorocebus aethiopsmedicineAnimalsHumansSecretionVero CellsVibrio choleraeCell DeathCytotoxinsHemolysinAnti-Bacterial AgentsVibrio choleraeVacuolesCytolysinMacrolidesIntracellular
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Effects ofBacillus thuringiensisCry1Ab and Cry3Aa endotoxins on predatory Coleoptera tested through artificial diet-incorporation bioassays

2009

AbstractTraditional approaches to studying the effects of genetically modified (GM) crops on beneficial insects involve either field assays, comparing insect population levels between control and GM crops or tritrophic bioassays with contaminated insects – usually larvae or eggs of Lepidoptera – as preys. Here, we report the results of a bioassay using an artificial diet, suitable for predatory Coleoptera, to supplyBacillus thuringiensis(Bt) solubilized Cry1Ab and Cry3Aa as well as trypsin-activated Cry1Ab toAtheta coriariaandCryptolaemus montrouzieriadults and young larvae ofAdalia bipunctata. Water, solubilization buffer and trypsin-treated solubilization buffer were used as controls. In …

Adalia bipunctataPopulationBacillus thuringiensisBiological pest controlMicrobiologyToxicologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisAnimalsBioassayBeneficial insectsCryptolaemus montrouzieriPest Control BiologicaleducationLarvaeducation.field_of_studyBacillus thuringiensis ToxinsbiologyfungiGeneral Medicinebiology.organism_classificationSurvival AnalysisDietColeopteraEndotoxinsLarvaPredatory BehaviorInsect ScienceBiological AssayAgronomy and Crop ScienceBulletin of Entomological Research
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Conductance and Ion Selectivity of a Mesoscopic Protein Nanopore Probed with Cysteine Scanning Mutagenesis

2005

Nanometer-scale proteinaceous pores are the basis of ion and macromolecular transport in cells and organelles. Recent studies suggest that ion channels and synthetic nanopores may prove useful in biotechnological applications. To better understand the structure-function relationship of nanopores, we are studying the ion-conducting properties of channels formed by wild-type and genetically engineered versions of Staphylococcus aureus alpha-hemolysin (alphaHL) reconstituted into planar lipid bilayer membranes. Specifically, we measured the ion selectivities and current-voltage relationships of channels formed with 24 different alphaHL point cysteine mutants before and after derivatizing the c…

AnionsModels MolecularStaphylococcus aureusCell Membrane PermeabilityBacterial ToxinsLipid BilayersAnalytical chemistryBiophysics02 engineering and technologyIonHemolysin ProteinsStructure-Activity Relationship03 medical and health sciencesCationsNanotechnologyCysteineChannels Receptors and Electrical SignalingLipid bilayerIon channel030304 developmental biologyIons0303 health sciencesChemistrySulfhydryl ReagentsConductance021001 nanoscience & nanotechnologyElectrostaticsElectrophysiologyNanoporeMembraneMutagenesisMutagenesis Site-DirectedBiophysicsGenetic Engineering0210 nano-technologySelectivityBiotechnologyBiophysical Journal
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Studies on the natural hemolytic system of the annelid worm Spirographis spallanzanii viviani (Polychaeta).

1981

Abstract Hemolytic activity in the hemolymph of Spirographis spallanzanii was estabilished against Bufo, sheep, calf, rabbit, rat, human A, B, O erythrocytes. Chemico-physical treatments suggest that the hemolytic factor could be a thermo-labile protein whose activity requires calcium ions and which is active over broad pH and temperature ranges. Some of these properties and the sigmoidal curve obtained by plotting the quantity of hemolymph against the percentage of hemolysis, produce some analogies with the mammalian lytic system.

AnnelidaImmunologychemistry.chemical_elementBiologyCalciumHemolysisHemolysin ProteinsHemolymphHemolymphmedicineAnimalsHumansMagnesiumHorsesSheepAnnelid wormTemperatureAnatomyHydrogen-Ion Concentrationmedicine.diseaseHemolysisBufonidaeRatschemistryBiochemistryCalciumCattleRabbitsChickensDevelopmental BiologyDevelopmental and comparative immunology
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Integrative Model for Binding of Bacillus thuringiensis Toxins in Susceptible and Resistant Larvae of the Diamondback Moth (Plutella xylostella)

1999

ABSTRACT Insecticidal crystal proteins from Bacillus thuringiensis in sprays and transgenic crops are extremely useful for environmentally sound pest management, but their long-term efficacy is threatened by evolution of resistance by target pests. The diamondback moth ( Plutella xylostella ) is the first insect to evolve resistance to B. thuringiensis in open-field populations. The only known mechanism of resistance to B. thuringiensis in the diamondback moth is reduced binding of toxin to midgut binding sites. In the present work we analyzed competitive binding of B. thuringiensis toxins Cry1Aa, Cry1Ab, Cry1Ac, and Cry1F to brush border membrane vesicles from larval midguts in a susceptib…

Bacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsApplied Microbiology and BiotechnologyBinding CompetitiveModels BiologicalHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalGeneticsBacillaceaeDiamondback mothBinding SitesEcologybiologyBacillus thuringiensis ToxinsParasporal bodyfungiPlutellafood and beveragesbiology.organism_classificationEndotoxinsCry1AcLarvaFood ScienceBiotechnology
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Production and characterization of Bacillus thuringiensis Cry1Ac-resistant cotton bollworm Helicoverpa zea (Boddie).

2007

ABSTRACT Laboratory-selected Bacillus thuringiensis -resistant colonies are important tools for elucidating B. thuringiensis resistance mechanisms. However, cotton bollworm, Helicoverpa zea , a target pest of transgenic corn and cotton expressing B. thuringiensis Cry1Ac (Bt corn and cotton), has proven difficult to select for stable resistance. Two populations of H. zea (AR and MR), resistant to the B. thuringiensis protein found in all commercial Bt cotton varieties (Cry1Ac), were established by selection with Cry1Ac activated toxin (AR) or MVP II (MR). Cry1Ac toxin reflects the form ingested by H. zea when feeding on Bt cotton, whereas MVP II is a Cry1Ac formulation used for resistance se…

Bacterial ToxinsBacillus thuringiensisMothsGossypiumApplied Microbiology and BiotechnologyCypermethrinInsecticide Resistancechemistry.chemical_compoundHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsPest Control BiologicalGossypiumGenetically modified maizeEcologybiologyBacillus thuringiensis Toxinsfungifood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticulturechemistryAgronomyCry1AcBt cottonHelicoverpa zeaPEST analysisFood ScienceBiotechnologyProtein BindingApplied and environmental microbiology
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Comparison of Different Methodologies for Binding Assays of Bacillus thuringiensis Toxins to Membrane Vesicles from Insect Midguts

2002

Bacterial ToxinsBacillus thuringiensisMothsSpodopteraHemolysin ProteinsCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanymedicineAnimalsEcology Evolution Behavior and SystematicsBacillaceaeBacillus thuringiensis ToxinsbiologyVesicleCell MembraneMidgutbiology.organism_classificationBacillalesEndotoxinsmedicine.anatomical_structureBiochemistryDigestive SystemBacteriaJournal of Invertebrate Pathology
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