Search results for "Clostridium Difficile"

showing 10 items of 65 documents

Clostridium difficile heterogeneously impacts intestinal community architecture but drives stable metabolome responses

2015

Clostridium difficile-associated diarrhoea (CDAD) is caused by C. difficile toxins A and B and represents a serious emerging health problem. Yet, its progression and functional consequences are unclear. We hypothesised that C. difficile can drive major measurable metabolic changes in the gut microbiota and that a relationship with the production or absence of toxins may be established. We tested this hypothesis by performing metabolic profiling on the gut microbiota of patients with C. difficile that produced (n=6) or did not produce (n=4) toxins and on non-colonised control patients (n=6), all of whom were experiencing diarrhoea. We report a statistically significant separation (P-value o0…

DiarrheaMaleBacterial ToxinsDiseasePathogenesisGut floraMicrobiologyMicrobiologyFecesClostridiumMetabolomicsRNA Ribosomal 16SmedicineMetabolomeHumansMetabolomicsColitisEcology Evolution Behavior and SystematicsbiologyClostridioides difficileClostridium difficilebiology.organism_classificationmedicine.diseaseColitisIntestinesRNA BacterialDiarrheaClostridium InfectionsMetabolomeFemaleOriginal Articlemedicine.symptomBacterial infection
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Characterization of the cleavage site and function of resulting cleavage fragments after limited proteolysis of Clostridium difficile toxin B (TcdB) …

2005

Clostridium difficiletoxin B (TcdB) is a single-stranded protein consisting of a C-terminal domain responsible for binding to the host cell membrane, a middle part involved in internalization, and the N-terminal catalytic (toxic) part. This study shows that TcdB is processed by a single proteolytic step which cleaves TcdB10463between Leu543and Gly544and the naturally occurring variant TcdB8864between Leu544and Gly545. The cleavage occurs at neutral pH and is catalysed by a pepstatin-sensitive protease localized in the cytoplasm and on the cytoplasmic face of intracellular membranes. The smaller N-terminal cleavage products [63 121 Da (TcdB10463) and 62 761 Da (TcdB8864)] harbour the cytotox…

Endosomemedia_common.quotation_subjectBacterial ToxinsMolecular Sequence DataClostridium difficile toxin BCleavage (embryo)MicrobiologyCricetulusBacterial ProteinsCricetinaeChlorocebus aethiopsAnimalsAmino Acid SequenceInternalizationLungVero CellsCells Culturedmedia_commonHost cell membraneClostridioides difficileChemistryFibroblastsMolecular biologyCytosolBiochemistryGlucosyltransferasesCytoplasmIntracellularPeptide HydrolasesSubcellular FractionsMicrobiology
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Liver infarction in a patient with Clostridium Difficile colitis. A possible connection?

2019

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Enterocolitismedicine.medical_specialtyFatal outcomebusiness.industryGastroenterologyClostridium difficileLiver infarctionGastroenterologyConnection (mathematics)Clostridium Difficile ColitisInternal medicinemedicinemedicine.symptombusinessJournal of Gastrointestinal and Liver Diseases
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Clostridium difficile IStron CdISt1: Discovery of a Variant Encoding Two Complete Transposase-Like Proteins

2004

ABSTRACT Screening a Clostridium difficile strain collection for the chimeric element Cd ISt1 , we identified two additional variants, designated Cd ISt1 -0 and Cd ISt1 -III. In in vitro assays, we could prove the self-splicing ribozyme activity of these variants. Structural comparison of all known Cd ISt1 variants led us to define four types of IStrons that we designated Cd ISt1 -0 through Cd ISt1 -III. Since Cd ISt1 -0 encodes two complete transposase-like proteins (TlpA and TlpB), we suggest that it represents the original genetic element, hypothesized before to have originated by fusion of a group I intron and an insertion sequence element.

Genetics0303 health sciencesbiology030306 microbiologyClostridioides difficileStrain (biology)Bacteriophages Transposons and PlasmidsMolecular Sequence DataRibozymeIntronTransposasesClostridium difficilebiology.organism_classificationMicrobiologyIntrons03 medical and health sciencesGenes Bacterialbiology.proteinBacteriologyDNA Transposable ElementsClostridiaceaeInsertion sequenceMolecular BiologyTransposase030304 developmental biology
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The IStron CdISt1 of Clostridium difficile: molecular symbiosis of a group I intron and an insertion element

2003

Abstract The IStron CdISt1 was first discovered as an insertion into the tcdA gene of the clinical isolate C34. It combines structural and functional properties of a group I intron at its 5′-end with those of an insertion element at its 3′-end. Up to date four different types could be found, mainly differing in their IS-element portions. Contrasting classical group I introns, CdISt1 is always integrated in ORFs encoding bacterial protein. In case CdISt1 had only the IS-element function such insertion would inactivate the protein encoded by the host gene. It is only due to the self-splicing activity of the group I intron parts that CdISt1 integration does not abolish protein function. Both e…

GeneticsInfectious DiseasesbiologySymbiosisIntronClostridium difficileORFSbiology.organism_classificationMicrobiologyGeneGenomeBacteriaFunction (biology)Anaerobe
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Characterization of polymorphisms in the toxin A and B genes of Clostridium difficile.

2006

We have used six independent polymerase chain reactions (A1–A3 and B1–B3) for amplification of the entire sequence of the two toxin genes tcdA and tcdB of several Clostridium difficile strains. With this approach we have detected (1) restriction site polymorphisms which are distributed all over the genes, and (2) deletions that could be found only in tcdA. Characteristic differences between strains were mainly focused to the 5′ third of tcdB (B1 fragment) and/or the 3′ third of tcdA (A3 fragment). The possible use of our approach for typing of C. difficile toxin genes is discussed.

GeneticsPolymorphism GeneticClostridioides difficileBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologyClostridium difficileMicrobiologyMolecular biologyPolymerase Chain Reactionlaw.inventionRestriction siteEnterotoxinsBacterial ProteinslawGenes BacterialGenotypeGeneticsTypingRestriction fragment length polymorphismMolecular BiologyPolymerase chain reactionPolymorphism Restriction Fragment LengthFEMS microbiology letters
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Clostridium difficile toxins A and B inhibit human immune response in vitro

1988

Two Clostridium difficile toxins isolated from strain VPI 10463 were tested for their effect on different human T-cell proliferation systems. In mitogen- and antigen-driven T-cell proliferation systems, toxins inhibited the proliferative response in a dose-dependent fashion. In interleukin-2-driven culture systems, no effect of toxins could be found on preactivated T cells. We suspected that monocytes were the influenced cells, since in antigen- and mitogen-driven systems monocytes were necessary for the proliferative response, whereas the interleukin-2-driven system was independent of monocytes. To prove this concept, purified monocytes were treated with toxins. The treatment was found to …

Interleukin 2Cellular immunityT-LymphocytesBacterial ToxinsImmunologyEnterotoxinIn Vitro TechniquesBiologyLymphocyte ActivationMicrobiologyMonocytesMicrobiologyEnterotoxinsImmune systemBacterial ProteinsAntigenmedicineHumansMonocytePseudomembranous colitisClostridium difficileInfectious Diseasesmedicine.anatomical_structureInterleukin-2ParasitologyMitogensResearch Articlemedicine.drugInfection and Immunity
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Rho protein inhibition blocks protein kinase C translocation and activation.

1998

Small GTP-binding proteins of the Ras and Rho family participate in various important signalling pathways. Large clostridial cytotoxins inactivate GTPases by UDP-glucosylation. Using Clostridium difficile toxin B-10463 (TcdB) for inactivation of Rho proteins (RhoA/Rac/Cdc42) and Clostridium sordellii lethal toxin-1522 (TcsL) for inactivation of Ras-proteins (Ras/Rac/Ral, Rap) the role of these GTPases in protein kinase C (PKC) stimulation was studied. Phorbol-myristate-acetate (PMA) induced a rapid PKC translocation to and activation in the particulate cell fraction as determined by PKC-activity measurements and Western blots for PKC alpha. These effects were blocked by TcdB inhibiting Rho …

LipopolysaccharidesRHOASwineBiophysicsClostridium difficile toxin ABronchiCell Cycle ProteinsGTPaseCDC42PKC alphaBiochemistryGTP-Binding ProteinsRHO protein GDP dissociation inhibitorAnimalsHumanscdc42 GTP-Binding ProteinMolecular BiologyProtein kinase CCells CulturedProtein Kinase CbiologyEpithelial CellsCell BiologyMolecular biologyCell biologyEnzyme ActivationCdc42 GTP-Binding Proteinbiology.proteinras ProteinsTetradecanoylphorbol AcetateEndothelium VascularrhoA GTP-Binding ProteinBiochemical and biophysical research communications
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Variant toxin B and a functional toxin A produced by Clostridium difficile C34.

2001

A particular property of Clostridium difficile strain C34 is an insertion of approximately 2 kb in the tcdA-C34 gene that does not hinder expression of a fully active TcdA-C34 molecule. Intoxication with TcdA-C34 induced an arborized appearance in eukaryotic cells (D-type cytopathic effect); intoxication with TcdB-C34 induced a spindle-like appearance of cells (S-type cytopathic effect). Inactivation of GTPases with purified toxins revealed that Rho, Rac, Cdc42, and Rap are substrates of TcdA-C34. The variant cytotoxin TcdB-C34 inactivated Rho, Rac, Cdc42, Rap, Ral, and R-Ras. Hence, this is the first ‘S-type’ cytotoxin which inactivates both Rho and R-Ras, and is coexpressed with a ‘D-type…

MaleCell SurvivalBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BGTPaseEnterotoxinCHO CellsBiologymedicine.disease_causeMicrobiologyMicrobiologyEnterotoxinsBacterial ProteinsCricetinaeGeneticsmedicineAnimalsHumansMolecular BiologyCells CulturedCytopathic effectSkinToxinClostridioides difficileCytotoxinsGenetic VariationClostridium difficileMolecular biologyCdc42 GTP-Binding ProteinDNA Transposable ElementsMicroscopy Electron ScanningFEMS microbiology letters
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Regulation of phospholipase D activity in synaptosomes permeabilized with Staphylococcus aureus alpha-toxin.

1998

In order to investigate the regulation of presynaptic phospholipase D (PLD) activity by calcium and G proteins, we established a permeabilization procedure for rat cortical synaptosomes using Staphylococcus aureus alpha-toxin (30-100 microg/ml). In permeabilized synaptosomes, PLD activity was significantly stimulated when the concentration of free calcium was increased from 0.1 microM to 1 microM. This activation was inhibited in the presence of KN-62 (1 microM), an inhibitor of calcium/calmodulin-dependent kinase II (CaMKII), but not by the protein kinase C inhibitor, Ro 31-8220 (1-10 microM). Synaptosomal PLD activity was also stimulated in the presence of 1 microM GTPgammaS. When Rho pro…

MaleStaphylococcus aureusCell Membrane PermeabilityG proteinBacterial ToxinsBiophysicschemistry.chemical_elementCalciumBiologyIn Vitro TechniquesBiochemistryClostridium difficile toxin Bchemistry.chemical_compoundHemolysin ProteinsStructural BiologyStaphylococcus aureus α-toxinCa2+/calmodulin-dependent protein kinaseSynaptosomeGeneticsPhospholipase DPhospholipase D activityAnimalsRats WistarMolecular BiologyProtein kinase CSynaptosomePhospholipase DRho proteinCalcium/calmodulin-dependent protein kinase IICell BiologyBrefeldin AMolecular biologyRatsEnzyme Activationenzymes and coenzymes (carbohydrates)BiochemistrychemistryGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)CalciumSynaptosomesFEBS letters
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