Search results for "Clostridium"

showing 10 items of 128 documents

Impact of probiotic Saccharomyces boulardii on the gut microbiome composition in HIV-treated patients: A double-blind, randomised, placebo-controlled…

2017

Dysbalance in gut microbiota has been linked to increased microbial translocation, leading to chronic inflammation in HIV-patients, even under effective HAART. Moreover, microbial translocation is associated with insufficient reconstitution of CD4+T cells, and contributes to the pathogenesis of immunologic non-response. In a double-blind, randomised, placebo-controlled trial, we recently showed that, compared to placebo, 12 weeks treatment with probiotic Saccharomyces boulardii significantly reduced plasma levels of bacterial translocation (Lipopolysaccharide-binding protein or LBP) and systemic inflammation (IL-6) in 44 HIV virologically suppressed patients, half of whom (n = 22) had immun…

RNA virusesMale0301 basic medicinePlacebo-controlled studylcsh:MedicineHIV InfectionsGut floraPathology and Laboratory MedicineSystemic inflammationlaw.inventionPlacebosProbiotic0302 clinical medicineImmunodeficiency ViruseslawMedicine and Health SciencesMedicinelcsh:ScienceImmune ResponseMultidisciplinarybiologyMicrobiotaGenomicsMiddle AgedProbiòticsBacterial PathogensIntestinesSaccharomyces boulardiiMedical MicrobiologyViral PathogensVirusesFemale030211 gastroenterology & hepatologyPathogensmedicine.symptomResearch ArticleSaccharomyces boulardiiAdultImmunologyMicrobial GenomicsMicrobiologySaccharomyces03 medical and health sciencesSigns and SymptomsImmune systemDouble-Blind MethodDiagnostic MedicineRetrovirusesGeneticsVIH (Virus)HumansMicrobiomeMicrobial PathogensInflammationClostridiumBacteriabusiness.industryProbioticsGut BacteriaLentivirusLachnospiraceaelcsh:ROrganismsFungiBiology and Life SciencesHIVbiology.organism_classificationYeast030104 developmental biologyImmunologylcsh:QMicrobiomebusinessPLoS ONE
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Rho protein-mediated changes in the structure of the actin cytoskeleton regulate human inducible NO synthase gene expression ☆ ☆This article contains…

2003

Rho proteins (Rho, Rac, Cdc 42) are known to control the organization of the actin cytoskeleton as well as gene expression. Inhibition of Rho proteins by Clostridium difficile toxin B disrupted the F-actin cytoskeleton and enhanced cytokine-induced inducible nitric oxide synthase (iNOS) expression in human epithelial cells. Also specific inhibition by Y-27632 of p160ROCK, which mediates Rho effects on actin fibers, caused a disruption of the actin cytoskeleton and a superinduction of cytokine-induced iNOS expression. Accordingly, direct disruption of the actin cytoskeleton by cytochalasin D, latrunculin B, or jasplakinolide enhanced cytokine-induced iNOS expression. The transcription factor…

Regulation of gene expressionActin remodelingClostridium difficile toxin Bmacromolecular substancesCell BiologyBiologyActin cytoskeletonMolecular biologyCell biologyProfilinSerum response factorbiology.proteinMDia1CytoskeletonExperimental Cell Research
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Effect of introduction of HACCP on the microbiological quality of some restaurant meals

2002

The microbial quality of Spanish potato omelette and pork loin before and after implementation of the HACCP system in University restaurants was used as indicator of food safety in this work. The prevalence of aerobic plate counts and incidences of Staphylococcus aureus, Escherichia coli, E. coli O157:H7, Listeria monocytogenes, Salmonella spp. and Clostridium perfringens were analysed. Results of implementation of the HACCP system show a lower incidence of studied microorganisms. On the other hand, a documented training in personal hygiene, good manufacturing practices (GMPs), cleaning and sanitation procedures and personal safety in addition to the rearrangement in the infrastructure of t…

SalmonellaSanitationbusiness.industryMicrobiological qualityClostridium perfringensmedicine.disease_causeFood safetyLower incidenceListeria monocytogenesPersonal hygienemedicineFood sciencebusinessFood ScienceBiotechnologyFood Control
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Assessment of microbial quality of commercial and home-made tiger-nut beverages

2012

Aims:  We aimed to assess the microbiological quality of Spanish commercial tiger-nut beverages as well as home-made samples collected from supermarkets, street vendors, juice bars and ice-cream parlours located in Valencia. Methods and Results:  Microbiological analysis of 44 tiger-nut beverages samples were carried out according to International Standard Organization (ISO) norms and published works which included the total viable count, Enterobacteriaceae, Escherichia coli, Staphylococcus aureus, Salmonella, Bacillus cereus, yeasts, moulds, Yersinia enterocolitca, Clostridium perfringens, Vibrio spp. and Listeria monocytogenes. The obtained results indicated that all the commercial sample…

SalmonellabiologySample (material)Bacillus cereusTotal Viable CountContaminationClostridium perfringensmedicine.disease_causebiology.organism_classificationApplied Microbiology and BiotechnologyListeria monocytogenesmedicineShigellaFood scienceLetters in Applied Microbiology
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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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Antibacterial effect of the bioactive compound beauvericin produced by Fusarium proliferatum on solid medium of wheat.

2010

To obtain the bioactive compound beauvericin (BEA), Fusarium proliferatum CECT 20569 was grown on a solid medium of wheat, utilizing the technique of the solid state fermentation (SSF), being this mycotoxin purified by high performance liquid chromatography (HPLC) with a reverse phase semi-preparative column using as the mobile phase acetonitrile/water in gradient condition. The purity of the BEA was verified by analytical HPLC and liquid chromatography tandem mass spectrometry (LC/MS-MS). The pure fractions of BEA were utilized to determinate the antibiotic effects on several bacterial strains that are considered normally pathogens of the intestinal tract as: Escherichia coli, Enterococcus…

Spectrometry Mass Electrospray IonizationFusarium proliferatumToxicologymedicine.disease_causeHigh-performance liquid chromatographymycotoxinchemistry.chemical_compoundFusariumTandem Mass SpectrometryLiquid chromatography–mass spectrometryDepsipeptideswheatmedicineTriticumAntibacterial agentChromatographybiologybeauvericinfood and beveragesClostridium perfringensbiology.organism_classificationBeauvericinBioactive compoundAnti-Bacterial AgentschemistrySolid-state fermentationSpectrophotometry UltravioletChromatography Liquid
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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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Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
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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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