Search results for " Toxins"

showing 10 items of 330 documents

Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate.

1996

Receptor signalling to phospholipase D (PLD) in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor apparently involves Rho proteins. Since phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] has been recognized as an essential cofactor for PLD activity and since activated Rho proteins have been reported to stimulate the synthesis of PtdIns(4,5)P2, we studied whether in HEK cells PLD activity is regulated by PtdIns(4,5)P2 and, in particular, whether PtdIns(4,5)P2 can restore PLD activity inhibited by Clostridium difficile toxin B, which inactivates Rho proteins. Addition of MgATP to permeabilized HEK cells increased basal PLD activity and potentia…

Phosphatidylinositol 45-DiphosphateGTP'Bacterial ToxinsClostridium difficile toxin BBiologyBiochemistryCell Linechemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsPhosphatidylcholineRhoB GTP-Binding ProteinPhospholipase DHumansPhosphatidylinositolEnzyme InhibitorsrhoB GTP-Binding ProteinPhospholipase DClostridioides difficileHEK 293 cellsCell MembraneMembrane ProteinsReceptors MuscarinicCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)chemistryPhosphatidylinositol 45-bisphosphateGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)European journal of biochemistry
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Control of cellular phosphatidylinositol 4,5-bisphosphate levels by adhesion signals and Rho GTPases in NIH 3T3 fibroblasts

2000

The involvement of small GTPases of the Rho family in the control of phosphoinositide metabolism by adhesion signals was examined in NIH 3T3 fibroblasts. Abrogation of adhesion signals by detachment of cells from their substratum resulted in a time-dependent decrease in the cellular level of PtdIns(4,5)P2 by approximately 50%. This effect could be mimicked by treatment of adherent cells with Clostridium difficile toxin B and toxin B-1470, which inhibit specific subsets of Rho and Ras GTPases. Detachment of cells that had been pretreated with the clostridial toxins did not cause a further reduction in PtdIns(4,5)P2 levels, suggesting that the target GTPases are integrated into the control of…

Phosphatidylinositol 45-Diphosphaterac1 GTP-Binding Proteinrho GTP-Binding ProteinsBacterial ToxinsCellClostridium difficile toxin BRAC1GTPasePhospholipaseBiologyTransfectionBiochemistryMicechemistry.chemical_compoundPhosphoinositide Phospholipase CBacterial ProteinsCell AdhesionmedicineAnimalsPhosphorylationInositol phosphatechemistry.chemical_classificationPhospholipase CCytotoxinsPhosphoric Diester Hydrolases3T3 CellsMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphotransferases (Alcohol Group Acceptor)medicine.anatomical_structurechemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesCalciumSignal TransductionEuropean Journal of Biochemistry
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A new gene superfamily of pathogen-response (repat) genes in Lepidoptera: Classification and expression analysis

2012

Repat (REsponse to PAThogens) genes were first identified in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae) in response to Bacillus thuringiensis and baculovirus exposure. Since then, additional repat gene homologs have been identified in different studies. In this study the comprehensive larval transcriptome from S. exigua was analyzed for the presence of novel repat-homolog sequences. These analyses revealed the presence of at least 46 repat genes in S. exigua, establishing a new gene superfamily in this species. Phylogenetic analysis and studies of conserved motifs in these hypothetical proteins have allowed their classification in two main classes, αREPAT and βREPAT. Studies o…

PhysiologyBacillus thuringiensisGenes InsectSpodopteradigestive systemBiochemistryTranscriptomeHemolysin ProteinsBacterial ProteinsBacillus thuringiensisGene expressionExiguaAnimalsMolecular BiologyGeneGeneticsBacillus thuringiensis ToxinsbiologyGene Expression ProfilingStem CellsfungiMidgutbiology.organism_classificationMolecular biologyEndotoxinsIntestinesLepidopteraGene expression profilingLarvaMetagenomeComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Mannose phosphate isomerase isoenzymes in Plutella xylostella support common genetic bases of resistance to Bacillus thuringiensis toxins in Llpidopt…

2001

ABSTRACT A strong correlation between two mannose phosphate isomerase (MPI) isoenzymes and resistance to Cry1A toxins from Bacillus thuringiensis has been found in a Plutella xylostella population. MPI linkage to Cry1A resistance had previously been reported for a Heliothis virescens population. The fact that the two populations share similar biochemical, genetic, and cross-resistance profiles of resistance suggests the occurrence of homologous resistance loci in both species.

PopulationBacterial ToxinsBacillus thuringiensisDrug ResistanceIsomeraseApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalseducationPest Control BiologicalGeneticseducation.field_of_studyMannose-6-Phosphate IsomeraseEcologyHeliothis virescensbiologyBacillus thuringiensis ToxinsMannose phosphate isomeraseParasporal bodyfungiPlutellaMannose-6-Phosphate Isomerasebiology.organism_classificationEndotoxinsIsoenzymesLepidopteraElectrophoresis Polyacrylamide GelFood ScienceBiotechnologyApplied and environmental microbiology
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Genetic and Biochemical Characterization of Field-Evolved Resistance to Bacillus thuringiensis Toxin Cry1Ac in the Diamondback Moth, Plutella xyloste…

2004

ABSTRACT The long-term usefulness of Bacillus thuringiensis Cry toxins, either in sprays or in transgenic crops, may be compromised by the evolution of resistance in target insects. Managing the evolution of resistance to B. thuringiensis toxins requires extensive knowledge about the mechanisms, genetics, and ecology of resistance genes. To date, laboratory-selected populations have provided information on the diverse genetics and mechanisms of resistance to B. thuringiensis , highly resistant field populations being rare. However, the selection pressures on field and laboratory populations are very different and may produce resistance genes with distinct characteristics. In order to better…

PopulationBacterial ToxinsBacillus thuringiensisGenetically modified cropsBiologyMothsApplied Microbiology and BiotechnologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisGenetic variationBotanyInvertebrate MicrobiologyAnimalsSelection GeneticeducationPest Control BiologicalCrosses GeneticGeneticseducation.field_of_studyDiamondback mothEcologyBacillus thuringiensis ToxinsMicrovillifungiPlutellaGenetic Variationbiology.organism_classificationEndotoxinsCry1AcPlutellidaeLarvaFood ScienceBiotechnology
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Pore-forming toxins activate MAPK p38 by causing loss of cellular potassium.

2009

Mitogen activated protein kinase (MAPK) p38 has emerged as a survival protein in cells that are attacked by bacterial toxins forming small membrane pores. Activation of p38 by pore forming toxins (PFT) has been attributed to osmotic stress, but here we show that loss of K+ is likely to be the critical parameter. Several lines of evidence support this conclusion: first, osmoprotection did not prevent p38-phosphorylation in alpha-toxin-loaded cells. Second, treatment of cells with a K+ ionophore, or simple incubation in K+-free medium sufficed to cause robust p38-phosphorylation. Third, media containing high [K+] prevented p38-activation by Staphylococcus aureus alpha-toxin, Vibrio cholerae c…

Pore Forming Cytotoxic ProteinsOsmotic shockp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologyHemolysin ProteinsBiochemistryp38 Mitogen-Activated Protein KinasesCell LineCell membraneHemolysin ProteinsmedicineHumansPhosphorylationMolecular BiologyPore-forming toxinEscherichia coli ProteinsCell MembraneHemolysinEpithelial CellsCell BiologyCell biologyEnzyme Activationmedicine.anatomical_structureBiochemistryPotassiumStreptolysinCalciumCytolysinBiochemical and biophysical research communications
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Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal α-toxin into the lipid bilayer

1995

Staphylococcal alpha-toxin is a primarily hydrophilic molecule that binds as a monomer to target membranes and then aggregates to form amphiphilic oligomers that represent water-filled transmembrane channels. Current evidence indicates that a region located in the center of the molecule inserts deeply into the bilayer. In the present study, we sought to determine whether membrane insertion was triggered by the oligomerization process, and whether insertion correlated with pore formation. Double mutants of alpha-toxin were prepared in which His-35 was replaced by Arg, and cysteine residues were introduced at positions 69, 130 and 186. Substitution of His-35 with Arg rendered the toxin molecu…

Pore formationBacterial ToxinsLipid BilayersMolecular ConformationBiophysics(Staphylococcus)Arginineα-ToxinBiochemistryHemolysin ProteinsMembrane Lipidschemistry.chemical_compound2-NaphthylamineAmphiphileOligomerizationCysteineLipid bilayerFluorescent DyesTransmembrane channelsPore-forming toxinBilayerCell BiologyMembraneMonomerchemistryBiochemistryMutationPore-forming toxinBiophysicsMembrane insertionCysteineBiochimica et Biophysica Acta (BBA) - Biomembranes
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Novel path to apoptosis: small transmembrane pores created by staphylococcal alpha-toxin in T lymphocytes evoke internucleosomal DNA degradation.

1994

Peripheral-blood human T lymphocytes were treated with Staphylococcus aureus alpha-toxin. Membrane permeabilization was assessed by measuring efflux of K+ and Rb+ and influx of Na+, Ca2+, and propidium iodide. Cellular ATP and [3H]thymidine incorporation following lectin stimulation were measured as parameters for cell viability. Internucleosomal cleavage characteristic of programmed cell death was assessed by agarose gel electrophoresis and by quantifying low-molecular-weight, [3H]thymidine-labeled DNA fragments. Nanomolar concentrations of alpha-toxin evoked protracted, irreversible ATP depletion in both activated and resting T lymphocytes. Toxin-damaged cells also lost their ability to i…

Programmed cell deathCell Membrane PermeabilityStaphylococcusT-LymphocytesImmunologyBacterial ToxinsApoptosisBiologyMicrobiologychemistry.chemical_compoundHemolysin ProteinsAdenosine TriphosphateHumansPropidium iodideViability assaySodiumT lymphocyteDNANucleosomesInfectious DiseaseschemistryBiochemistryApoptosisAgarose gel electrophoresisBiophysicsPotassiumParasitologyCalciumThymidineAdenosine triphosphateResearch Article
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Interferons increase cell resistance to Staphylococcal alpha-toxin.

2007

ABSTRACTMany bacterial pathogens, includingStaphylococcus aureus, use a variety of pore-forming toxins as important virulence factors. Staphylococcal alpha-toxin, a prototype β-barrel pore-forming toxin, triggers the release of proinflammatory mediators and induces primarily necrotic death in susceptible cells. However, whether host factors released in response to staphylococcal infections may increase cell resistance to alpha-toxin is not known. Here we show that prior exposure to interferons (IFNs) prevents alpha-toxin-induced membrane permeabilization, the depletion of ATP, and cell death. Moreover, pretreatment with IFN-α decreases alpha-toxin-induced secretion of interleukin 1β (IL-1β)…

Programmed cell deathStaphylococcus aureusCell Membrane Permeabilitymedicine.medical_treatmentImmunologyBacterial ToxinsInterleukin-1betaBiologyStaphylococcal infectionsMicrobiologyProinflammatory cytokineMicrobiologyCell LineHemolysin ProteinsAdenosine TriphosphateInterferonmedicineHumansSecretionCell DeathKinaseEpithelial CellsBacterial Infectionsmedicine.diseaseInfectious DiseasesCytokineProtein BiosynthesisParasitologyTumor necrosis factor alphaInterferonsFatty Acid Synthasesmedicine.drugInfection and immunity
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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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