Search results for "vibrio cholerae"

showing 10 items of 28 documents

Exploring relationships between drought and epidemic cholera in Africa using generalised linear models

2021

Abstract Background Temperature and precipitation are known to affect Vibrio cholerae outbreaks. Despite this, the impact of drought on outbreaks has been largely understudied. Africa is both drought and cholera prone and more research is needed in Africa to understand cholera dynamics in relation to drought. Methods Here, we analyse a range of environmental and socioeconomic covariates and fit generalised linear models to publicly available national data, to test for associations with several indices of drought and make cholera outbreak projections to 2070 under three scenarios of global change, reflecting varying trajectories of CO2 emissions, socio-economic development, and population gr…

EpidemiologyPopulationClimate changeInfectious and parasitic diseasesRC109-216MicrobiologyCholera1108 Medical Microbiologyparasitic diseasesmedicinePopulation growthClimate changeHumansScenario analysisSocioeconomicseducationEpidemicsDisease outbreaksVibrio choleraeSustainable developmenteducation.field_of_studyPublic healthResearchOutbreakfood and beverages1103 Clinical SciencesGlobal changemedicine.diseaseCholeraDroughtsInfectious DiseasesGeographyVDP::Medisinske Fag: 700::Helsefag: 800AfricaLinear Models0605 MicrobiologyBMC Infectious Diseases
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Accessing sub-national cholera epidemiological data for Nigeria and the Democratic Republic of Congo during the seventh pandemic.

2022

Abstract Background Vibrio cholerae is a water-borne pathogen with a global burden estimate at 1.4 to 4.0 million annual cases. Over 94% of these cases are reported in Africa and more research is needed to understand cholera dynamics in the region. Cholera data are lacking, mainly due to reporting issues, creating barriers for widespread research on cholera epidemiology and management in Africa. Main body Here, we present datasets that were created to help address this gap, collating freely available sub-national cholera data for Nigeria and the Democratic Republic of Congo. The data were collated from a variety of English and French publicly available sources, including the World Health Or…

EpidemiologyVDP::Medisinske Fag: 700::Helsefag: 800::Epidemiologi medisinsk og odontologisk statistikk: 803Nigeria1103 Clinical SciencesDemocratic Republic of CongoMicrobiologyUnited StatesInfectious DiseasesCholera1108 Medical MicrobiologyDemocratic Republic of the CongoHumansVDP::Medisinske Fag: 700Public HealthPandemicsVibrio cholerae0605 MicrobiologyBMC infectious diseases
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Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: a TEM study.

2002

The Vibrio cholerae cytolysin (VCC) 63-kDa monomer has been shown to interact in aqueous suspension with cholesterol microcystals to produce a ring/pore-like heptameric oligomer approximately 8 nm in outer diameter. Transmission electron microscopy data were produced from cholesterol samples adsorbed to carbon support films, spread across the holes of holey carbon films, and negatively stained with ammonium molybdate. The VCC oligomers initially attach to the edge of the stacked cholesterol bilayers and with increasing time cover the two planar surfaces. VCC oligomers are also released into solution, with some tendency to cluster, possibly via the hydrophobic membrane-spanning domain. At th…

ErgosterolLiposomeCytotoxinsTemperatureOligomerNegative stainProtein Structure TertiaryCrystallographychemistry.chemical_compoundMicroscopy ElectronMonomerCholesterolchemistryPulmonary surfactantModels ChemicalStructural BiologySide chainImage Processing Computer-Assistedlipids (amino acids peptides and proteins)CytolysinCholesterol EstersVibrio choleraeFluorescent DyesJournal of structural biology
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Phobalysin, a Small β-Pore-Forming Toxin of Photobacterium damselae subsp. damselae

2015

ABSTRACT Photobacterium damselae subsp. damselae , an important pathogen of marine animals, may also cause septicemia or hyperaggressive necrotizing fasciitis in humans. We previously showed that hemolysin genes are critical for virulence of this organism in mice and fish. In the present study, we characterized the hlyA gene product, a putative small β-pore-forming toxin, and termed it phobalysin P (PhlyP), for “photobacterial lysin encoded on a plasmid.” PhlyP formed stable oligomers and small membrane pores, causing efflux of K + , with no significant leakage of lactate dehydrogenase but entry of vital dyes. The latter feature distinguished PhlyP from the related Vibrio cholerae cytolysin…

ErythrocytesBacterial ToxinsMolecular Sequence DataImmunologyVirulencemedicine.disease_causeHemolysin ProteinsHemolysisMicrobiologyBacterial AdhesionMicrobiologyHemolysin ProteinsmedicineAnimalsHumansAmino Acid SequencePore-forming toxinbiologyPhotobacteriumEpithelial CellsHemolysinPhotobacteriumbiology.organism_classificationMolecular PathogenesisInfectious DiseasesPhotobacterium damselaeVibrio choleraeParasitologyRabbitsCytolysinSequence AlignmentInfection and Immunity
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Genome size reduction through multiple events of gene disintegration in Buchnera APS

2001

The evolution of the endosymbiont Buchnera during its adaptation to intracellular life involved a massive reduction in its genome. By comparing the orthologous genes of Buchnera, Escherichia coli and Vibrio cholerae, we show that the minimal genome size of Buchnera arose from multiple events of gene disintegration dispersed over the whole genome. The elimination of the genes was a continuous process that began with gene inactivation and progressed until the DNA corresponding to the pseudogenes were completely deleted.

GeneticsGenome evolutionPseudogeneBacterial genome sizebiochemical phenomena metabolism and nutritionBiologybiology.organism_classificationBiological EvolutionGenomeBuchneraEscherichia coliGeneticsMinimal genomeBuchneraVibrio choleraeGeneGenome sizeGene DeletionGenome BacterialPseudogenesTrends in Genetics
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Picomolar inhibition of cholera toxin by a pentavalent ganglioside GM1os-calix[5]arene

2013

Cholera toxin (CT), the causative agent of cholera, displays a pentavalent binding domain that targets the oligosaccharide of ganglioside GM1 (GM1os) on the periphery of human abdominal epithelial cells. Here, we report the first GM1os-based CT inhibitor that matches the valency of the CT binding domain (CTB). This pentavalent inhibitor contains five GM1os moieties linked to a calix[5]arene scaffold. When evaluated by an inhibition assay, it achieved a picomolar inhibition potency (IC50 = 450 pM) for CTB. This represents a significant multivalency effect, with a relative inhibitory potency of 100000 compared to a monovalent GM1os derivative, making GM1os-calix[5]arene one of the most potent…

Models MolecularCholera ToxinbindingStereochemistrydesignCalix[5]areneEpithelial cellsG(M1) GangliosideHeat-labile enterotoxinmedicine.disease_causeligandBiochemistrycrystalMultivalency effectsCholeraCausative agentsmedicinePotencyHumansoligosaccharidePhysical and Theoretical ChemistryIC50Vibrio choleraeheat-labile enterotoxinVLAGchemistry.chemical_classificationgm1 mimicsGangliosideInhibition assaysChemistryCholera toxinOrganic ChemistryOligosaccharideBinding domainLigand (biochemistry)ValenciesOrganische ChemiehexamethylenetetramineChemistryPositive ionsaffinityAntitoxinsCalixarenesrecognitionBinding domain
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Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as beta-barrel toxins from gram-positive organisms.

2009

Vibrio cholerae cytolysin (VCC) forms SDS-stable heptameric beta-barrel transmembrane pores in mammalian cell membranes. In contrast to structurally related pore formers of gram-positive organisms, no oligomeric prepore stage of assembly has been detected to date. In the present study, disulfide bonds were engineered to tie the pore-forming amino acid sequence to adjacent domains. In their nonreduced form, mutants were able to bind to rabbit erythrocytes and to native erythrocyte membranes suspended in PBS solution and form SDS-labile oligomers. These remained nonfunctional and represented the long-sought VCC prepores. Disulfide bond reduction in these oligomers released the pore-forming se…

Models MolecularPore Forming Cytotoxic ProteinsMutantBiologyIn Vitro Techniquesmedicine.disease_causeGram-Positive BacteriaBiochemistryModels Biologicalchemistry.chemical_compoundProtein structureGeneticsmedicineAnimalsCysteineProtein Structure QuaternaryMolecular BiologyPeptide sequenceVibrio choleraeCytotoxinsErythrocyte MembraneTransmembrane proteinRecombinant ProteinsMonomerMembraneBiochemistrychemistryVibrio choleraeMutagenesis Site-DirectedCytolysinRabbitsBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells

1997

Many strains of Vibrio cholerae non-O1 and O1 El Tor that cause diarrhea do not harbor genes for a known secretogenic toxin. However, these strains usually elaborate a pore-forming toxin, hitherto characterized as a hemolysin and here designated V. cholerae cytolysin, whose action on intestinal cells has not yet been described. We report that V. cholerae cytolysin binds as a monomer to Intestine 407 cells and then assembles into detergent-stable oligomers that probably represent tetra- or pentamers. Oligomer formation is accompanied by generation of small transmembrane pores that allow rapid flux of K+ but not influx of Ca2+ or propidium iodide. Pore formation is followed by irreversible AT…

Nuclear EnvelopeImmunologymedicine.disease_causeMicrobiologyEl TorMicrobiologychemistry.chemical_compoundVibrionaceaemedicineHumansPropidium iodideVibrio choleraeCells CulturedIon TransportCell DeathbiologyCytotoxinsToxinCell MembraneHemolysinbiology.organism_classificationIntestinesInfectious DiseaseschemistryVibrio choleraeCell cultureParasitologyCytolysinResearch ArticleInfection and Immunity
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Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane

2007

Vibrio cholerae cytolysin (VCC) forms oligomeric transmembrane pores in cholesterol-rich membranes. To better understand this process, we used planar bilayer membranes. In symmetric membranes, the rate of the channel formation by VCC has a superlinear dependency on the cholesterol membrane fraction. Thus, more than one cholesterol molecule can facilitate VCC-pore formation. In asymmetric membranes, the rate of pore formation is limited by the leaflet with the lower cholesterol content. Methyl-beta-cyclodextrin, which removes cholesterol from membranes, rapidly inhibits VCC pore formation, even when it is added to the side opposite that of VCC addition. The results suggest that cholesterol i…

Pore Forming Cytotoxic Proteinsgenetic structuresLipid BilayersBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundMonolayermedicineAnimalsMoleculeVibrio choleraePore-forming toxinMembrane GlycoproteinsPerforinCholesterolbeta-CyclodextrinsGeneral Medicineeye diseasesTransmembrane proteinCholesterolMembraneBiochemistrychemistryVibrio choleraeBiophysicsCattlelipids (amino acids peptides and proteins)sense organsCytolysinBiochimie
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Mode of primary binding to target membranes and pore formation induced by Vibrio cholerae cytolysin (hemolysin).

1997

Vibrio cholerae cytolysin (VCC) is produced by many non-choleratoxigenic strains of V. cholerae, and possibly represents a relevant pathogenicity determinant of these bacteria. The protein is secreted as a pro-toxin that is proteolytically cleaved to yield the active toxin with a molecular mass of approximately 63 kDa. We here describe a simple procedure for preparative isolation of mature VCC from bacterial culture supernatants, and present information on its mode of binding and pore formation in biological membranes. At low concentrations, toxin monomers interact with a high-affinity binding site on highly susceptible rabbit erythrocytes. This as yet unidentified binding site is absent on…

Pore-forming toxinBinding SitesToxinCytotoxinsErythrocyte MembraneMolecular Sequence DataAerolysinHemolysinBiologymedicine.disease_causeBiochemistryTransmembrane proteinMolecular WeightBiochemistryVibrio choleraemedicineAnimalsHumansCytolysinAmino Acid SequenceRabbitsBinding siteVibrio choleraeEuropean journal of biochemistry
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