Search results for "Cholera"

showing 10 items of 67 documents

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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Polycondensed nitrogen heterocycles. Part17. Isoxazolo[4,3-d]pyrazolo[3,4-f][1,2,3]triazepine. A new ring system

1987

The title compounds were prepared by nitration of compounds 2, reduction of the dinitro derivatives 4 and diazotization of the diamino derivatives 6 followed by an intramolecular coupling reaction. Compound 4a showed good activity against Salmonella cholerasuis and Clostridium perfringens bacteria.

Organic Chemistrychemistry.chemical_elementNuclear magnetic resonance spectroscopyClostridium perfringensmedicine.disease_causeRing (chemistry)NitrogenCoupling reactionSalmonella cholerasuischemistry.chemical_compoundchemistryIntramolecular forceNitrationmedicineOrganic chemistryJournal of Heterocyclic Chemistry
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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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Cholesterol Specificity of Some Heptameric β-Barrel Pore-Forming Bacterial Toxins: Structural and Functional Aspects

2010

Apart from the thiol-specific/cholesterol-dependent cytolysin family of toxins (see Chapter 20) there are a number of other unrelated bacterial toxins that also have an affinity for plasma membrane cholesterol. Emphasis is given here on the Vibrio cholerae cytolysin (VCC) and the cytolysins from related Vibrio species. The inhibition of the cytolytic activity of these toxins by prior incubation with extracellular cholesterol or low density lipoprotein emerges as a unifying feature, as does plasma membrane cholesterol depletion. Incubation of VCC with cholesterol produces a heptameric oligomer, which is not equivalent to the pre-pore since it is unable to penetrate the plasma membrane. In st…

Pore-forming toxinHemolysinmedicine.disease_causeOligomerchemistry.chemical_compoundMembranechemistryBiochemistryVibrio choleraeLow-density lipoproteinExtracellularmedicinelipids (amino acids peptides and proteins)Cytolysin
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Using self-controlled case series to understand the relationship between conflict and cholera in Nigeria and the Democratic Republic of Congo

2021

Abstract Background Cholera outbreaks contribute significantly to diarrhoeal disease mortality, especially in low-income countries. Cholera outbreaks have several social and environmental risk factors and extreme conditions can act as catalysts for outbreaks. A social extreme with known links to infectious disease outbreaks is conflict, causing disruption to services, loss of income and displacement. Methods Here, we explored this relationship in Nigeria and the Democratic Republic of Congo (DRC), by fitting publicly available cholera and conflict data to conditional logistic regression models. We used the self-controlled case series method in a novel application, to understand if an exposu…

Povertybusiness.industrymedia_common.quotation_subjectAbsolute risk reductionOutbreakmedicine.diseaseCholeraDemocracyGeographyConflict resolutionHealth caremedicinebusinessSocioeconomicsInternational developmentmedia_common
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A cellular metalloproteinase activates Vibrio cholerae pro-cytolysin.

2004

Many strains of Vibrio cholerae produce a cytolysin (VCC) that forms oligomeric transmembrane pores in animal cells. The molecule is secreted as a procytolysin (pro-VCC) of 79 kDa that must be cleaved at the N terminus to generate the active 65-kDa toxin. Processing can occur in solution, and previous studies have described the action of mature VCC thus generated. However, little is known about the properties of pro-VCC itself. In this study, it is shown that pro-VCC exist as a monomer in solution and binds as a monomer to eukaryotic cells. Bound pro-VCC can then be activated either by exogenous, extracellular, or by endogenous, cell-bound proteases. In both cases, cleavage generates the 65…

ProteasesCholera Toxingenetic structuresCHO CellsBiologyADAM17 Proteinmedicine.disease_causeBiochemistryMiceCricetinaemedicineADAM17 ProteinAnimalsHumansProtein PrecursorsMolecular BiologyFurinMetalloproteinaseCytotoxinsCell MembraneMetalloendopeptidasesCell BiologyADAM Proteinseye diseasesTransmembrane proteinADAM ProteinsBiochemistryVibrio choleraebiology.proteinsense organsCytolysinRabbitsThe Journal of biological chemistry
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Mapping geographical inequalities in oral rehydration therapy coverage in low-income and middle-income countries, 2000-17

2020

Background: Oral rehydration solution (ORS) is a form of oral rehydration therapy (ORT) for diarrhoea that has the potential to drastically reduce child mortality; yet, according to UNICEF estimates, less than half of children younger than 5 years with diarrhoea in low-income and middle-income countries (LMICs) received ORS in 2016. A variety of recommended home fluids (RHF) exist as alternative forms of ORT; however, it is unclear whether RHF prevent child mortality. Previous studies have shown considerable variation between countries in ORS and RHF use, but subnational variation is unknown. This study aims to produce high-resolution geospatial estimates of relative and absolute coverage o…

RJ101medicine.medical_treatmentCHILDRENZINC0302 clinical medicine030212 general & internal medicinemedia_commonGeographylcsh:Public aspects of medicine1. No povertyLow income and middle income countriesGeneral Medicine3142 Public health care science environmental and occupational health3. Good healthPeer reviewGeographyChild PreschoolA990 Medicine and Dentistry not elsewhere classifiedGeographical inequalities0605 MicrobiologyDiarrheaAFRICAInequalityDEATHSmedia_common.quotation_subject030231 tropical medicineDeveloping countryArticleRS1117 Public Health and Health Services03 medical and health sciencesMORBIDITYEnvironmental healthDIARRHEAL DISEASEmedicineHumansOral rehydration therapyHealthcare DisparitiesDeveloping CountriesModels StatisticalCHOLERAMORTALITYInfant NewbornInfantlcsh:RA1-1270Bayes TheoremMiddle incomeGLOBAL BURDENChild mortality0605 Microbiology 1117 Public Health and Health ServicesHealth Care SurveysITC-ISI-JOURNAL-ARTICLEFluid TherapyNAHuman medicineITC-GOLD
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B subunits of cholera toxin and thermolabile enterotoxin of Escherichia coli have similar adjuvant effect as whole molecules on rotavirus 2/6-VLP spe…

2015

The purpose of this study was to evaluate the adjuvant effect of the B subunits of cholera toxin (CT) and the thermolabile enterotoxin of Escherichia coli (LT) by the intrarectal route of immunization and compare them to the whole molecules CT and LT-R192G, a non toxic mutant of LT, using 2/6-VLP as an antigen, in mice. All molecules induced similar antigen specific antibody titers in serum and feces, whereas different T cell profiles were observed. CTB and LTB, conversely to CT and LT-R192G, did not induce detectable production of IL-2 by antigen specific T cells. Moreover, CTB, conversely to LT-R192G, CT and LTB, did not induce antigen specific CD4+CD25+Foxp3- and Foxp3+ T cells, thus sho…

RotavirusCholera Toxin[SDV]Life Sciences [q-bio]T cellmedicine.medical_treatmentBacterial ToxinsEnterotoxinBiologymedicine.disease_causeAntibodies ViralMicrobiologyAntibodiesMicrobiologyB subunitEnterotoxinsFecesMiceAntigenAdjuvants ImmunologicImmunologicAdministration RectalmedicineAnimalsViralAdjuvantsIL-2 receptorVaccines Virus-Like ParticleThermolabileB cellVaccinesIntrarectalEscherichia coli ProteinsCholera toxinRotavirus VaccinesLT-R192G3. Good healthVirus-Like ParticleInfectious Diseasesmedicine.anatomical_structureAdministrationAntibody FormationInterleukin-2Th17 CellsImmunizationRectalAdjuvantImmunologic MemoryMicrobial pathogenesis
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