Search results for "bacterial toxin"

showing 10 items of 192 documents

Assessment of the Antimicrobial Activity and the Entomocidal Potential of Bacillus thuringiensis Isolates from Algeria.

2017

This work represents the first initiative to analyze the distribution of B. thuringiensis in Algeria and to evaluate the biological potential of the isolates. A total of 157 isolates were recovered, with at least one isolate in 94.4% of the samples. The highest Bt index was found in samples from rhizospheric soil (0.48) and from the Mediterranean area (0.44). Most isolates showed antifungal activity (98.5%), in contrast to the few that had antibacterial activity (29.9%). A high genetic diversity was made evident by the finding of many different crystal shapes and various combinations of shapes within a single isolate (in 58.4% of the isolates). Also, over 50% of the isolates harbored cry1, …

0301 basic medicineAntifungalStaphylococcus aureusmedicine.drug_classHealth Toxicology and Mutagenesis030106 microbiologyBacterial ToxinsBiological pest controlBacillus thuringiensisBiologyToxicologyArticleMicrobiology03 medical and health sciencesB. thuringiensisAnti-Infective AgentsBacterial ProteinsBacillus thuringiensismedicineEscherichia colibiocontrolGeneSoil MicrobiologyGenetic diversitycryChitinasesFungi<i>B. thuringiensis</i>; antibacterial; antifungal; <i>cry</i>; <i>vip3</i>; chitinase; biocontrolAntimicrobialbiology.organism_classificationCryptochromesantibacterialHexosaminidasesGenes BacterialAlgeriachitinaseChitinasePseudomonas aeruginosavip3biology.proteinMicroscopy Electron ScanningAntibacterial activityantifungalToxins
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Repair of a Bacterial Small β-Barrel Toxin Pore Depends on Channel Width

2017

ABSTRACT Membrane repair emerges as an innate defense protecting target cells against bacterial pore-forming toxins. Here, we report the first paradigm of Ca2+-dependent repair following attack by a small β-pore-forming toxin, namely, plasmid-encoded phobalysin of Photobacterium damselae subsp. damselae. In striking contrast, Vibrio cholerae cytolysin, the closest ortholog of phobalysin, subverted repair. Mutational analysis uncovered a role of channel width in toxicity and repair. Thus, the replacement of serine at phobalysin´s presumed channel narrow point with the bulkier tryptophan, the corresponding residue in Vibrio cholerae cytolysin (W318), modulated Ca2+ influx, lysosomal exocytosi…

0301 basic medicineBacterial ToxinsAerolysinmedicine.disease_causeMicrobiologySerine03 medical and health sciencesNanoporesVirologyExtracellularmedicineHumansVibrio choleraeChemistryToxinPerforinCell MembraneQR1-502Transmembrane proteinCell biology030104 developmental biologyPhotobacterium damselaeVibrio choleraeCalciumCytolysinResearch ArticlemBio
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Staphylococcus aureus α-toxin: small pore, large consequences

2018

Abstract The small β-pore-forming α-toxin, also termed α-hemolysin or Hla is considered to be an important virulence factor of Staphylococcus aureus. Perforation of the plasma membrane (PM) by Hla leads to uncontrolled flux of ions and water. Already a small number of toxin pores seems to be sufficient to induce complex cellular responses, many of which depend on the efflux of potassium. In this article, we discuss the implications of secondary membrane lesions, for example, by endogenous channels, for Hla-mediated toxicity, for calcium-influx and membrane repair. Activation of purinergic receptors has been proposed to be a major contributor to the lytic effects of various pore forming prot…

0301 basic medicineCell Membrane PermeabilityStaphylococcal ToxoidBacterial ToxinsClinical BiochemistryPerforation (oil well)Endocytosismedicine.disease_causeBiochemistryVirulence factorHemolysin Proteins03 medical and health sciencesCytosol0302 clinical medicinemedicineHumansMolecular BiologyPore-forming toxinIon TransportChemistryToxinCell MembranePurinergic receptorCell biologyCytosol030104 developmental biologyCalciumEffluxProtein Kinases030217 neurology & neurosurgeryBiological Chemistry
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Grey Matter Microstructural Integrity Alterations in Blepharospasm Are Partially Reversed by Botulinum Neurotoxin Therapy.

2016

OBJECTIVE Benign Essential Blepharospasm (BEB) and hemifacial spasm (HFS) are the most common hyperkinetic movement disorders of facial muscles. Although similar in clinical presentation different pathophysiological mechanisms are assumed. Botulinum Neurotoxin (BoNT) is a standard evidence-based treatment for both conditions. In this study we aimed to assess grey matter microstructural differences between these two groups of patients and compared them with healthy controls. In patients we furthermore tracked the longitudinal morphometric changes associated with BoNT therapy. We hypothesized microstructural differences between the groups at the time point of maximum symptoms representation a…

0301 basic medicineCentral Nervous SystemMaleMovement disordersBotulinum ToxinsBlepharospasmlcsh:MedicineToxicologyPathology and Laboratory MedicineNervous SystemDiagnostic Radiology0302 clinical medicineMaterials PhysicsMedicine and Health SciencesToxinsLongitudinal StudiesGray Matterlcsh:ScienceMicrostructureMultidisciplinaryMovement DisordersRadiology and ImagingPhysicsMotor CortexBrainNeurodegenerative DiseasesAnatomyMiddle AgedMagnetic Resonance ImagingPathophysiologyBotulinum neurotoxinFacial musclesDystoniamedicine.anatomical_structureTreatment OutcomeNeurologyPhysical SciencesFemalePrimary motor cortexmedicine.symptomAnatomyResearch ArticleAdultmedicine.medical_specialtyImaging TechniquesBlepharospasmToxic AgentsBacterial ToxinsMaterials ScienceBotulinum ToxinGrey matterResearch and Analysis Methods03 medical and health sciencesDiagnostic MedicineOphthalmologymedicineHumansHemifacial SpasmDemographyAgedbusiness.industrylcsh:RBiology and Life SciencesCorrectionmedicine.disease030104 developmental biologyCross-Sectional StudiesFacePeople and Placeslcsh:QbusinessHead030217 neurology & neurosurgeryHemifacial spasmPloS one
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Enterocyte Purge and Rapid Recovery Is a Resilience Reaction of the Gut Epithelium to Pore-Forming Toxin Attack.

2016

International audience; Besides digesting nutrients, the gut protects the host against invasion by pathogens. Enterocytes may be subjected to damage by both microbial and host defensive responses, causing their death. Here, we report a rapid epithelial response that alleviates infection stress and protects the enterocytes from the action of microbial virulence factors. Intestinal epithelia exposed to hemolysin, a pore-forming toxin secreted by Serratia marcescens, undergo an evolutionarily conserved process of thinning followed by the recovery of their initial thickness within a few hours. In response to hemolysin attack, Drosophila melanogaster enterocytes extrude most of their apical cyto…

0301 basic medicineCytoplasmDisease toleranceSurvivalApoptosismedicine.disease_causeOral infectionHemolysin ProteinsLipid droplet[SDV.IDA]Life Sciences [q-bio]/Food engineeringMitochondrial extrusionIntestinal MucosaSerratia marcescensBacterial-infectionPore-forming toxinbiologyCell DeathMicrovilliPlasma-membrane[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringGut EpitheliumMitochondriamedicine.anatomical_structureDrosophila melanogasterEnterocyteVirulence FactorsVarroidaeSerratia-marcescensBacterial ToxinsVirulenceMicrobiologyMicrobiologySerratia Infections03 medical and health sciencesVirologymedicineAnimalsApical cytoplasmDefense strategyDrosophila cyclin jToxinbiology.organism_classificationLipid dropletsDisease Models AnimalIntestinal Diseases030104 developmental biologyEnterocytesSerratia marcescensParasitologyDigestive SystemCell hostmicrobe
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Insecticidal Activity and Synergistic Combinations of Ten Different Bt Toxins against Mythimna separata (Walker)

2018

The oriental armyworm (OAW), Mythimna separata (Walker), is a destructive pest of agricultural crops in Asia and Australia. Commercialized Bt crops have performed very well against their target pests

0301 basic medicineInsecticidesHealth Toxicology and MutagenesisBacterial ToxinsBacillus thuringiensislcsh:MedicineVip3 proteinMothsToxicologymedicine.disease_causeArticleMicrobiology03 medical and health sciencesMythimna separataBacillus thuringiensis<i>Bacillus thuringiensis</i>medicineAnimalsBioassayPotencyCry proteinbiologyToxinlcsh:Rfungifood and beveragesDrug Synergismbiology.organism_classification030104 developmental biologyCry1AcLarvaoriental armywormPEST analysisBacteriaToxins
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Correction for Chakroun et al., Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

2016

Entomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no …

0301 basic medicineInsecticidesInsectaProtein ConformationBacterial ToxinsDrug ResistanceReviewsProtein EngineeringMicrobiology03 medical and health sciencesBacterial ProteinsBotanyTable (landform)AnimalsAmino Acid SequenceAuthor CorrectionPest Control BiologicalMolecular BiologyConserved SequencebiologyBacteriafungibiology.organism_classificationPlants Genetically Modified030104 developmental biologyInfectious DiseasesBacteria
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Susceptibility, mechanisms of response and resistance to Bacillus thuringiensis toxins in Spodoptera spp.

2016

Bioinsecticides based on Bacillus thuringiensis have long been used as an alternative to synthetic insecticides to control insect pests. In this review, we focus on insects of the genus Spodoptera, including relevant polyphagous species that are primary and secondary pests of many crops, and how B. thuringiensis toxins can be used for Spodoptera spp. pest management. We summarize the main findings related to susceptibility, midgut binding specificity, mechanisms of response and resistance of this insect genus to B. thuringiensis toxins.

0301 basic medicineIntegrated pest managementResistance (ecology)media_common.quotation_subjectBacterial ToxinsfungiBacillus thuringiensisfood and beveragesMidgutInsectSpodopteraBiologySpodopterabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciences030104 developmental biologyInsect ScienceBacillus thuringiensisBotanyAnimalsEcology Evolution Behavior and Systematicsmedia_commonCurrent Opinion in Insect Science
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Recombinant anthrax protective antigen: Observation of aggregation phenomena by TEM reveals specific effects of sterols.

2017

Abstract Negatively stained transmission electron microscope images are presented that depict the aggregation of recombinant anthrax protective antigen (rPA83 monomer and the PA63 prepore oligomer) under varying in vitro biochemical conditions. Heat treatment (50 °C) of rPA83 produced clumped fibrils, but following heating the PA63 prepore formed disordered aggregates. Freeze-thaw treatment of the PA63 prepore generated linear flexuous aggregates of the heptameric oligomers. Aqueous suspensions of cholesterol microcrystals were shown to bind small rPA83 aggregates at the edges of the planar bilayers. With PA63 a more discrete binding of the prepores to the crystalline cholesterol bilayer ed…

0301 basic medicineModels MolecularHot TemperatureBacterial ToxinsGeneral Physics and AstronomyFibrilOligomerNegative Staining03 medical and health scienceschemistry.chemical_compoundProtein AggregatesMicroscopy Electron TransmissionStructural BiologyFreezingGeneral Materials ScienceAntigens BacterialAqueous solutionChemistryBilayerCell BiologyHydrogen-Ion ConcentrationNegative stainSterolRecombinant ProteinsCrystallographySterols030104 developmental biologyMonomerCholesterolTransmission electron microscopyCrystallizationDeoxycholic AcidMicron (Oxford, England : 1993)
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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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