Search results for "Clostridioides"

showing 7 items of 37 documents

The Enterotoxin from Clostridium difficile (ToxA) Monoglucosylates the Rho Proteins

1995

The enterotoxin from Clostridium difficile (ToxA) is one of the causative agents of the antibiotic-associated pseudomembranous colitis. In cultured monolayer cells ToxA exhibits cytotoxic activity to induce disassembly of the actin cytoskeleton, which is accompanied by morphological changes. ToxA-induced depolymerization of actin filaments is correlated with a decrease in the ADP-ribosylation of the low molecular mass GTP-binding Rho proteins (Just, I., Selzer, J., von Eichel-Streiber, C., and Aktories, K. (1995) J. Clin. Invest. 95, 1026-1031). Here we report on the identification of the ToxA-induced modification of Rho. Applying electrospray mass spectrometry, the mass of the modification…

RHOAGlycoside HydrolasesBacterial ToxinsClostridium difficile toxin ARAC1macromolecular substancesEnterotoxinBiochemistrySubstrate SpecificityEnterotoxinsGTP-Binding ProteinsTumor Cells CulturedAmino AcidsMolecular BiologyActinbiologyMolecular massClostridioides difficileCell BiologyPseudomembranous colitisActin cytoskeletonMolecular biologycarbohydrates (lipids)GlucoseBiochemistrybiology.proteinrhoA GTP-Binding ProteinJournal of Biological Chemistry
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Inhibition of FcεRI-mediated Activation of Rat Basophilic Leukemia Cells by Clostridium difficile Toxin B (Monoglucosyltransferase)

1996

Abstract Treatment of rat basophilic leukemia (RBL) 2H3-hm1 cells with Clostridium difficile toxin B (2 ng/ml), which reportedly depolymerizes the actin cytoskeleton, blocked [3H]serotonin release induced by 2,4-dinitrophenyl-bovine serum albumin, carbachol, mastoparan, and reduced ionophore A23187-stimulated degranulation by about 55-60%. In lysates of RBL cells, toxin B 14C-glucosylated two major and one minor protein. By using two-dimensional gel electrophoresis and immunoblotting, RhoA and Cdc42 were identified as protein substrates of toxin B. In contrast to toxin B, Clostridium botulinum transferase C3 that selectively inactivates RhoA by ADP-ribosylation did not inhibit degranulation…

SerotoninRHOABacterial ToxinsClostridium difficile toxin AWasp VenomsClostridium difficile toxin BBiologyCytoplasmic GranulesTritiummedicine.disease_causeBiochemistryCell LinePhosphatidylinositol 3-KinasesBacterial ProteinsTumor Cells CulturedmedicineAnimalsEnzyme InhibitorsMolecular BiologyCalcimycinAdenosine Diphosphate RiboseClostridioides difficileReceptors IgEToxinDegranulationSerum Albumin BovineCell BiologyActin cytoskeletonMolecular biologyRatsAndrostadienesKineticsPhosphotransferases (Alcohol Group Acceptor)Leukemia Basophilic AcuteBiochemistryGlucosyltransferasesMastoparanbiology.proteinIntercellular Signaling Peptides and ProteinsClostridium botulinumCarbacholCattle24-DinitrophenolPeptidesWortmanninDinitrophenolsJournal of Biological Chemistry
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Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B

1995

Strain 1470 is the standard typing strain for serogroup F of Clostridium difficile containing both toxin genes, toxA-1470 and toxB-1470. A polymerase chain reaction (PCR)-based approach to the sequencing of the total toxB-1470 gene identified an open reading frame (ORF) of 7104 nucleotides. In comparison with the previously sequenced toxB of C. difficile VP10463, the toxB-1470 gene has 16 additional nucleotides, 13 within the 5'-untranslated region and three within the coding region. The M(r) of ToxB-1470 is 269,262, with an isoelectric point (IP) of 4.16. The equivalent values for ToxB are M(r) 269,709 and IP 4.13. In comparison with ToxB, ToxB-1470 differs primarily in the N-terminal regi…

SwineSequence analysisBacterial ToxinsMolecular Sequence DataRestriction MappingClostridium sordelliiMicrobiologyCell LineMicrobiologyOpen Reading FramesBacterial ProteinsAnimalsCoding regionAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceGeneClostridiumBase SequencebiologyClostridioides difficileCytotoxinsSequence Analysis DNAClostridium difficileClostridium novyibiology.organism_classificationActinsOpen reading frameGenes BacterialEndothelium VascularMolecular Microbiology
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Glucosylation of Rho proteins by Clostridium difficile toxin B.

1995

TOXIN A and B, the major virulence factors of Clostridium difficile, are the causative agents of antibiotic-associated pseudomembran-ous colitis. In cultured cell lines their potent cytotoxicity results from their ability to induce disaggregation of the microfilament cytoskeleton1,2. Toxin B acts on the low-molecular-mass GTPase Rho A3,4, which is involved in the regulation of the actin cytoskeleton. We report here that toxin B catalyses the incorporation of up to one mole of glucose per mole of RhoA at the amino acid thre-onine at position 37. The modification was identified and localized by tandem electrospray mass spectrometry. UDP-glucose selectively serves as cosubstrate for the monogl…

ThreonineRHOAGlycosylationBacterial ToxinsMolecular Sequence DataClostridium difficile toxin AClostridium difficile toxin Bmacromolecular substancesmedicine.disease_causeMicrofilamentCatalysisMass SpectrometryGTP PhosphohydrolasesBacterial ProteinsGTP-Binding ProteinsmedicineTumor Cells CulturedAnimalsAmino Acid SequenceCytoskeletonActinCells CulturedCytoskeletonMultidisciplinarybiologyToxinClostridioides difficileActin cytoskeletonActinsRecombinant ProteinsRatsGlucoseMarsupialiaBiochemistryGlucosyltransferasesbiology.proteinrhoA GTP-Binding ProteinNature
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The actin-based motility of intracellularListeria monocytogenesis not controlled by small GTP-binding proteins of the Rho- and Ras-subfamilies

1999

In this study, we analyzed whether the actin-based motility of intracellular Listeria monocytogenes is controlled by the small GTP-binding proteins of the Rho- and Ras-subfamilies. These signalling proteins are key regulatory elements in the control of actin dynamics and their activity is essential for the maintenance of most cellular microfilament structures. We used the Clostridium difficile toxins TcdB-10463 and TcdB-1470 to specifically inactivate these GTP-binding proteins. Treatment of eukaryotic cells with either of these toxins led to a dramatic breakdown of the normal actin cytoskeleton, but did not abrogate the invasion of epithelial cells by L. monocytogenes and had no effect on …

Time FactorsArp2/3 complexClostridium difficile toxin Bmacromolecular substancesBiologyMicrofilamentMicrobiologyCell LineBacterial ProteinsGTP-Binding ProteinsGeneticsMolecular BiologyMicroscopy ConfocalMicroscopy VideoClostridioides difficileActin remodelingActin cytoskeletonListeria monocytogenesActinsCell biologyEndotoxinsProfilinParacytophagyMicroscopy Electron Scanningras Proteinsbiology.proteinMDia1FEMS Microbiology Letters
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UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii.

1996

Abstract We have previously isolated a fibroblast mutant cell with high resistance to the two Rho-modifying glucosyltransferase toxins A and B of Clostridium difficile. We demonstrate here a low level of UDP-glucose in the mutant, which explains its toxin resistance since: (i) to obtain a detectable toxin B-mediated Rho modification in lysates of mutant cells, addition of UDP-glucose was required, and it promoted the Rho modification dose-dependently; (ii) high pressure liquid chromatography analysis of nucleotide extracts of cells indicated that the level of UDP-glucose in the mutant (0.8 nmol/106 cells) was lower than in the wild type (3.7 nmol/106 cells); and (iii) sensitivity to toxin B…

Uridine Diphosphate GlucoseMicroinjectionsMutantBacterial ToxinsClostridium difficile toxin AClostridium sordelliiClostridium difficile toxin Bmedicine.disease_causeBiochemistryMicrobiologyCell LineCricetulusBacterial ProteinsGTP-Binding ProteinsCricetinaemedicineAnimalsMolecular BiologyClostridiumbiologyToxinClostridioides difficileWild typeCell BiologyClostridium difficilebiology.organism_classificationGlucosyltransferasesMutationbiology.proteinGlucosyltransferaseThe Journal of biological chemistry
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Alimentary and Pharmaceutical Approach to Natural Antimicrobials against Clostridioides difficile Gastrointestinal Infection

2021

Incidence of Clostridioides difficile infection (CDI) has been increasing in recent decades due to different factors, namely (i) extended use of broad-spectrum antibiotics, (ii) transmission within asymptomatic and susceptible patients, and (iii) unbalanced gastrointestinal microbiome and collateral diseases that favor C. difficile gastrointestinal domination and toxin production. Although antibiotic therapies have resulted in successful control of CDI in the last 20 years, the development of novel strategies is urged in order to combat the capability of C. difficile to generate and acquire resistance to conventional treatments and its consequent proliferation. In this regard, vegetable and…

medicine.medical_specialtyHealth (social science)genetic structuresmedicine.drug_classAntibioticsDietary supplementPlant ScienceTP1-1185Health Professions (miscellaneous)Microbiology<i>Clostridioides difficile</i>03 medical and health sciencesfucoidanmedicineMicrobiomeIntensive care medicine030304 developmental biologyalgae0303 health sciences030306 microbiologybusiness.industryTransmission (medicine)marine bioactivesChemical technologyGastrointestinal MicrobiomeAntimicrobialnatural antimicrobialsbusinessdietClostridioidesFood ScienceFoods
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