Search results for "vibrio cholerae"

showing 10 items of 28 documents

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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2017

Coastal marine Vibrio cholerae populations usually exhibit high genetic diversity. To assess the genetic diversity of abundant V. cholerae non-O1/non-O139 populations in the Central European lake Neusiedler See, we performed a phylogenetic analysis based on recA, toxR, gyrB and pyrH loci sequenced for 472 strains. The strains were isolated from three ecologically different habitats in a lake that is a hot-spot of migrating birds and an important bathing water. We also analyzed 76 environmental and human V. cholerae non-O1/non-O139 isolates from Austria and other European countries and added sequences of seven genome-sequenced strains. Phylogenetic analysis showed that the lake supports a un…

0301 basic medicineGenetic diversityPhylogenetic treeEcology030106 microbiologyBiologymedicine.disease_causeMicrobiologyGenetic recombination03 medical and health sciencesMonophylyVibrio choleraePhylogeneticsGenetic variationmedicineCladeEcology Evolution Behavior and SystematicsEnvironmental Microbiology
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Wild eel microbiome reveals that skin mucus of fish could be a natural niche for aquatic mucosal pathogen evolution

2017

Background Fish skin mucosal surfaces (SMS) are quite similar in composition and function to some mammalian MS and, in consequence, could constitute an adequate niche for the evolution of mucosal aquatic pathogens in natural environments. We aimed to test this hypothesis by searching for metagenomic and genomic evidences in the SMS-microbiome of a model fish species (Anguilla Anguilla or eel), from different ecosystems (four natural environments of different water salinity and one eel farm) as well as the water microbiome (W-microbiome) surrounding the host. Results Remarkably, potentially pathogenic Vibrio monopolized wild eel SMS-microbiome from natural ecosystems, Vibrio anguillarum/Vibr…

0301 basic medicineMicrobiology (medical)DNA BacterialVibrio anguillarumGenomic IslandsZoologyAnimals WildVibrio vulnificusmedicine.disease_causeMicrobiologylcsh:Microbial ecologyEvolution Molecular03 medical and health sciencesMicrobial ecologymedicineAnimalsHumansMicrobiomeVibrioSkin mucusSkinbiologyBacteriaResearchMicrobiotaAttached microbiotaGenomicsbiology.organism_classificationAnguillaPathogenicity islandMucusVibrioMucusGenòmica030104 developmental biologyVibrio choleraeBacteris patògenslcsh:QR100-130MicrobiomeMetagenomicsWater Microbiology
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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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New insights regarding Acinetobacter genomic island-related elements

2020

The objective of this study was to mobilize the Acinetobacter genomic island 1-A (AGI1-A) from Enterobacter hormaechei EclCSP2185 (E. cloacae complex) and to search for the distribution and structure of AGI1-related elements in the NCBI database. AGI1-A was transferred to Escherichia coli. Analysis of the attachment (att) sites could locate the possible recombination crossover in the att sequences at position 10-11 (GG) in the last 18 bp of trmE. In silico detection of AGI backbones in the wgs database identified AGI variants in Salmonella enterica (83 strains), Vibrio cholerae (33), E. hormaechei (12), Acinetobacter baumannii (2), most belonging to prevalent clones (ST40, ST69, ST114 and S…

Acinetobacter baumanniiDNA Bacterial0301 basic medicineMicrobiology (medical)Genomic IslandsKlebsiella pneumoniae[SDV]Life Sciences [q-bio]030106 microbiologyEnterobactermedicine.disease_causeIntegronIntegrons03 medical and health sciences0302 clinical medicineDrug Resistance Multiple BacterialGenomic islandEscherichia colimedicineHumansPharmacology (medical)030212 general & internal medicineProteus mirabilisVibrio choleraeEscherichia coliGeneticsbiologySalmonella entericaSequence Analysis DNAGeneral MedicineAcinetobacterbiology.organism_classificationAnti-Bacterial AgentsAcinetobacter baumanniiInfectious DiseasesSalmonella entericaVibrio choleraebiology.protein
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Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric …

2003

AbstractMembrane cholesterol is essential to the activity of at least two structurally unrelated families of bacterial pore-forming toxins, represented by streptolysin O (SLO) and Vibrio cholerae cytolysin (VCC), respectively. Here, we report that SLO and VCC differ sharply in their interaction with liposome membranes containing enantiomeric cholesterol (ent-cholesterol). VCC had very low activity with ent-cholesterol, which is in line with a stereospecific mode of interaction of this toxin with cholesterol. In contrast, SLO was only slightly less active with ent-cholesterol than with cholesterol, suggesting a rather limited degree of structural specificity in the toxin–cholesterol interact…

Cell Membrane Permeabilitygenetic structuresBiophysicsBiologymedicine.disease_causeBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsStructural Biologyotorhinolaryngologic diseasesGeneticsmedicineStreptolysin OMolecular BiologyVibrio cholerae030304 developmental biology0303 health sciencesLiposomeVibrio cholerae cytolysinCholesterolToxinCytotoxinsEnantiomeric cholesterol030302 biochemistry & molecular biologyMembranes ArtificialStereoisomerismCell BiologyFluoresceinseye diseasesRecombinant ProteinsCholesterol-binding cytolysinsMembraneCholesterolchemistryBiochemistryVibrio choleraeLiposomesStreptolysinsProtein–cholesterol interactionlipids (amino acids peptides and proteins)Streptolysinsense organsCytolysinEnantiomerProtein BindingFEBS letters
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Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target memb…

1999

Vibrio cholerae cytolysin permeabilizes animal cell membranes. Upon binding to the target lipid bilayer, the protein assembles into homo-oligomeric pores of an as yet unknown stoichiometry. Pore formation has been observed with model liposomes consisting of phosphatidylcholine and cholesterol, but the latter were much less susceptible to the cytolysin than were erythrocytes or intestinal epithelial cells. We here show that liposome permeabilization is strongly promoted if cholesterol is combined with sphingolipids, whereby the most pronounced effects are observed with monohexosylceramides and free ceramide. These two lipid species are prevalent in mammalian intestinal brush border membranes…

CeramideCell Membrane PermeabilityPentamerProtein ConformationGalactosylceramidesBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundPhosphatidylcholinemedicineHumansLipid bilayerMolecular BiologyVibrio choleraeCells CulturedLiposomeSphingolipidsCytotoxinsBrainCell BiologyFluoresceinsLipid MetabolismMembraneCholesterolBiochemistrychemistryVibrio choleraeLiposomesElectrophoresis Polyacrylamide GelCytolysinIsoelectric FocusingThe Journal of biological chemistry
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Coupling of Cholesterol and Cone-shaped Lipids in Bilayers Augments Membrane Permeabilization by the Cholesterol-specific Toxins Streptolysin O and V…

2001

Abstract Vibrio cholerae cytolysin (VCC) forms oligomeric pores in lipid bilayers containing cholesterol. Membrane permeabilization is inefficient if the sterol is embedded within bilayers prepared from phosphatidylcholine only but is greatly enhanced if the target membrane also contains ceramide. Although the enhancement of VCC action is stereospecific with respect to cholesterol, we show here that no such specificity applies to the two stereocenters in ceramide; all four stereoisomers of ceramide enhanced VCC activity in cholesterol-containing bilayers. A wide variety of ceramide analogs were as effective asd-erythro-ceramide, as was diacylglycerol, suggesting that the effect of ceramide …

Cholera ToxinCeramideCell Membrane PermeabilityLipid BilayersBiologyCeramidesBiochemistrychemistry.chemical_compoundBacterial ProteinsPhosphatidylcholineLipid bilayerNuclear Magnetic Resonance BiomolecularVibrio choleraeMolecular BiologyDiacylglycerol kinaseCytotoxinsCell BiologyLipid MetabolismLipidsSphingolipidSterolCholesterolchemistryBiochemistryStreptolysinslipids (amino acids peptides and proteins)StreptolysinCytolysinJournal of Biological Chemistry
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R plasmids in environmental Vibrio cholerae non-O1 strains.

1988

The occurrence of drug resistance and its plasmid-mediated transferability was investigated in 140 environmental strains of Vibrio cholerae non-O1 and 6 strains of Vibrio cholerae, both O1 and non-O1, of clinical origin. Of the 146 strains tested, 93% were resistant to at least one drug and 74% were resistant to two or more antibiotics. The O1 strains were susceptible to all antibiotics used. A total of 26 of 28 selected resistant wild strains carried R plasmids that were transferable by intraspecific and intergeneric matings. The most common transmissible R factor determined resistance to ampicillin, amoxicillin, and sulfanilamide (30%), followed by resistance to ampicillin and amoxicillin…

DNA BacterialR FactorsFresh WaterDrug resistancemedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyPlasmidVibrio cholerae non-O1VibrionaceaeAmpicillinmedicineSeawaterVibrio choleraeElectrophoresis Agar GelEcologybiologyVirulenceGenetic transferDrug Resistance MicrobialSulfanilamidebiology.organism_classificationAnti-Bacterial AgentsVibrio choleraeConjugation GeneticWater MicrobiologyFood ScienceBiotechnologymedicine.drugResearch Article
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Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fl…

2000

AbstractHemolytic strains of Vibrio cholerae secrete a cytolysin that, upon binding as a monomer, forms pentameric pores in animal cell membranes. Pore formation is inhibited at low temperature and in the absence of cholesterol. We here posed the following questions: firstly, can oligomerization be observed in the absence of pore formation? Secondly, is membrane fluidity responsible for the effect of temperature or of cholesterol upon pore formation? The first issue was approached by chemical cross-linking, by electrophoretic heteromer analysis, and by electron microscopy. None of these methods yielded any evidence of a non-lytic pre-pore oligomer. The second question was addressed by the u…

DiphenylhexatrieneCell Membrane PermeabilityMembrane permeabilityMembrane FluidityBacterial ToxinsBiophysicsPorinsFluorescence PolarizationBiologymedicine.disease_causePore forming toxinBiochemistrychemistry.chemical_compoundProtein oligomerizationBacterial ProteinsBacteriocinsmedicineMembrane fluidityProtein oligomerizationVibrio choleraePhospholipidsFluorescent DyesLiposomeCytotoxinsCell MembraneCell BiologyFluoresceinsCholesterolMembranechemistryBiochemistryVibrio choleraeLiposomesPhosphatidylcholinesCytolysinDiphenylhexatrieneBiochimica et Biophysica Acta (BBA) - Biomembranes
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