Search results for "Escher"

showing 10 items of 728 documents

Genetics for Pseudoalteromonas provides tools to manipulate marine bacterial virus PM2

2008

ABSTRACT The genetic manipulation of marine double-stranded DNA (dsDNA) bacteriophage PM2 ( Corticoviridae ) has been limited so far. The isolation of an autonomously replicating DNA element of Pseudoalteromonas haloplanktis TAC125 and construction of a shuttle vector replicating in both Escherichia coli and Pseudoalteromonas enabled us to design a set of conjugative shuttle plasmids encoding tRNA suppressors for amber mutations. Using a host strain carrying a suppressor plasmid allows the introduction and analysis of nonsense mutations in PM2. Here, we describe the isolation and characterization of a suppressor-sensitive PM2 sus2 mutant deficient in the structural protein P10. To infect an…

MESH: Corticoviridae[SDV]Life Sciences [q-bio]Bacteriophages Transposons and PlasmidsMutantPlasmidPseudoalteromonasRNA TransferMESH: Genetic VectorsMESH: Models GeneticMESH: Capsid ProteinsGenetics0303 health sciencesbiologyMESH: Escherichia coliPseudoalteromonasMESH: Mutagenesis Site-DirectedPhenotypeMESH: DNA CircularElectrophoresis Polyacrylamide GelDNA CircularMESH: Genome ViralPlasmidsMESH: MutationGenetic VectorsGenome ViralMESH: PhenotypeMicrobiologyPseudoalteromonas haloplanktisViral Proteins03 medical and health sciencesShuttle vectorMESH: PlasmidsHost outer membraneEscherichia coliSeawaterMolecular Biology030304 developmental biologyModels Genetic030306 microbiologyMESH: PseudoalteromonasCorticoviridaeMESH: SeawaterViral membranebiology.organism_classificationMESH: RNA TransferMESH: Viral Proteins[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyMutationMutagenesis Site-DirectedCapsid ProteinsBacterial virusMESH: Electrophoresis Polyacrylamide Gel
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Combined action of redox potential and pH on heat resistance and growth recovery of sublethally heat-damaged Escherichia coli

2000

International audience; The combined effect of redox potential (RP) (from -200 to 500 mV) and pH (from 5.0 to 7.0) on the heat resistance and growth recovery after heat treatment of Escherichia coli was tested. The effect of RP on heat resistance was very different depending on the pH. At pH 6.0, there was no significant difference, whereas at pH 5.0 and 7.0 maximum resistance was found in oxidizing conditions while it fell in reducing ones. In sub-lethally heat-damaged cells, low reducing and acid conditions allowed growth ability to be rapidly regained, but a decrease in the redox potential and pH brought about a longer lag phase and a slower exponential growth rate, and even led to growt…

MESH: Oxidation-ReductionMESH : Escherichia coliMESH: Hydrogen-Ion ConcentrationHot TemperatureThermal resistanceMESH: Hot Temperaturemedicine.disease_causeApplied Microbiology and BiotechnologyRedox03 medical and health sciencesExponential growthMESH : Hydrogen-Ion Concentration[ SDV.MP ] Life Sciences [q-bio]/Microbiology and ParasitologyOxidizing agentEscherichia colimedicineGrowth rate[INFO.INFO-BT]Computer Science [cs]/Biotechnology[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyEscherichia coliComputingMilieux_MISCELLANEOUS030304 developmental biologyMESH : Oxidation-Reduction0303 health sciencesbiologyMESH: Escherichia coli030306 microbiologyChemistryGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationEnterobacteriaceaeCulture Media[INFO.INFO-BT] Computer Science [cs]/Biotechnology[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryMESH: Culture MediaBiophysicsMESH : Culture MediaMESH : Hot TemperatureOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyBacteriaBiotechnologyApplied Microbiology and Biotechnology
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Changes in the proton-motive force in Escherichia coli in response to external oxidoreduction potential.

1999

International audience; The pH homeostasis and proton-motive force (Deltap) of Escherichia coli are dependent on the surrounding oxidoreduction potential (ORP). Only the internal pH value and, thus, the membrane pH gradient (DeltapH) component of the Deltap is modified, while the membrane potential (DeltaPsi) does not change in a significant way. Under reducing conditions (Eh < 50 mV at pH 7.0), E. coli decreases its Deltap especially in acidic media (21% decrease at pH 7.0 and 48% at pH 5.0 for a 850-mV ORP decrease). Measurements of ATPase activity and membrane proton conductance (CH+m) depending on ORP and pH have shown that the internal pH decrease is due to an increase in membrane prot…

MESH: Oxidation-ReductionMESH : Escherichia coliMESH: Hydrogen-Ion ConcentrationMembrane permeabilitymedicine.disease_causeBiochemistryMembrane Potentials03 medical and health sciencesMESH : Hydrogen-Ion Concentration[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologymedicineEscherichia coliMESH: Adenosine TriphosphatasesMESH : Membrane PotentialsMESH : ProtonsMESH: Membrane Potentials[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology[INFO.INFO-BT]Computer Science [cs]/Biotechnology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliComputingMilieux_MISCELLANEOUS030304 developmental biologyMESH : Oxidation-ReductionMembrane potentialchemistry.chemical_classificationAdenosine Triphosphatases0303 health sciencesChromatographyMESH : Adenosine Triphosphatases030306 microbiologyChemiosmosisChemistryMESH: Escherichia coliConductanceHydrogen-Ion Concentration[INFO.INFO-BT] Computer Science [cs]/BiotechnologyMembranePermeability (electromagnetism)BiophysicsThiolMESH: ProtonsProtonsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/Biotechnology
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Construction of Chimeric Dual-Chain Avidin by Tandem Fusion of the Related Avidins

2011

BackgroundAvidin is a chicken egg-white protein with high affinity to vitamin H, also known as D-biotin. Many applications in life science research are based on this strong interaction. Avidin is a homotetrameric protein, which promotes its modification to symmetrical entities. Dual-chain avidin, a genetically engineered avidin form, has two circularly permuted chicken avidin monomers that are tandem-fused into one polypeptide chain. This form of avidin enables independent modification of the two domains, including the two biotin-binding pockets; however, decreased yields in protein production, compared to wt avidin, and complicated genetic manipulation of two highly similar DNA sequences i…

Macromolecular Assemblieslcsh:MedicineBiosensing TechniquesPolymerase Chain ReactionBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureBiotinMacromolecular Structure AnalysisProtein biosynthesisBiomacromolecule-Ligand InteractionsSurface plasmon resonancelcsh:Science0303 health sciencesMultidisciplinarybiologyrespiratory systemRecombinant ProteinsBiochemistryBiotinylationChromatography GelBiophysic Al SimulationsResearch ArticleProtein StructureStructural similarityRecombinant Fusion Proteins030303 biophysicsBiophysicsBiotinMolecular Dynamics SimulationBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesstomatognathic systemDefense ProteinsEscherichia coliAnimalsGene familyProtein InteractionsBiology030304 developmental biologylcsh:RProteinsComputational BiologySurface Plasmon ResonanceAvidinchemistrySmall MoleculesFermentationbiology.proteinlcsh:QChickensAvidinPLoS ONE
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Role of meprins to protect ileal mucosa of Crohn's disease patients from colonization by adherent-invasive E. coli

2011

Ileal lesions in Crohn's disease (CD) patients are colonized by pathogenic adherent-invasive Escherichia coli (AIEC) able to adhere to and invade intestinal epithelial cells (IEC), and to survive within macrophages. The interaction of AIEC with IEC depends on bacterial factors mainly type 1 pili, flagella, and outer membrane proteins. In humans, proteases can act as host defence mechanisms to counteract bacterial colonization. The protease meprin, composed of multimeric complexes of the two subunits alpha and beta, is abundantly expressed in IECs. Decreased levels of this protease correlate with the severity of the inflammation in patients with inflammatory bowel disease. The aim of the pre…

MaleBacterial Diseasesmedicine.medical_treatmentACTIVATION MECHANISMBiochemistryBacterial AdhesionPilusMice0302 clinical medicineCrohn DiseaseIntestinal mucosaMolecular Cell BiologyGastrointestinal InfectionsIntestinal MucosaAged 80 and over0303 health sciencesMultidisciplinaryQRMetalloendopeptidasesMiddle AgedEnzymesBacterial Pathogens3. Good healthHost-Pathogen InteractionInfectious DiseasesCytokineESCHERICHIA-COLI030220 oncology & carcinogenesisAlimentation et NutritionMedicineFemaleINFLAMMATORY-BOWEL-DISEASE;INTESTINAL EPITHELIAL-CELLS;URINARY-TRACT-INFECTIONS;ESCHERICHIA-COLI;ALPHA-SUBUNIT;STRAIN LF82;METALLOPROTEASE MEPRIN;ACTIVATION MECHANISM;BETA-SUBUNIT;TYPE-1 PILICellular Typesmedicine.symptomBacterial outer membraneALPHA-SUBUNITResearch ArticleAdultProteasesScienceMédecine humaine et pathologieInflammationGastroenterology and HepatologyBiologyMETALLOPROTEASE MEPRINMicrobiologyMicrobiologyURINARY-TRACT-INFECTIONS03 medical and health sciencesTYPE-1 PILIEscherichia colimedicineAnimalsHumansFood and NutritionSecretionInterleukin 8BETA-SUBUNITBiologyAged030304 developmental biologySTRAIN LF82Interleukin-8Inflammatory Bowel DiseaseEpithelial Cellsdigestive system diseasesMice Inbred C57BLHuman health and pathologyINTESTINAL EPITHELIAL-CELLS[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyINFLAMMATORY-BOWEL-DISEASE
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Conformational Change in the Pheromone-binding Protein fromBombyx mori Induced by pH and by Interaction with Membranes

1999

The pheromone-binding protein (PBP) from Bombyx mori was expressed in Escherichia coli periplasm. It specifically bound radiolabeled bombykol, the natural pheromone for this species. It appeared as a single band both in native and SDS-polyacrylamide gel electrophoresis and was also homogeneous in most chromatographic systems. However, in ion-exchange chromatography, multiple forms sometimes appeared. Attempts to separate them revealed that they could be converted into one another. Analysis of the protein by circular dichroism and fluorescence spectroscopy demonstrated that its tertiary structure was sensitive to pH changes and that a dramatic conformational transition occurred between pH 6.…

MaleConformational changeCircular dichroismSensory Receptor CellsProtein ConformationBiochemistryBombykolchemistry.chemical_compoundEscherichia coliAnimalsDenaturation (biochemistry)Pheromone bindingCloning MolecularMolecular BiologyChemistryCircular DichroismCell BiologyHydrogen-Ion ConcentrationBombyxChromatography Ion ExchangeLigand (biochemistry)Protein tertiary structureProtein Structure TertiarySpectrometry FluorescenceBiochemistryBiophysicsInsect ProteinsIntercellular Signaling Peptides and ProteinsThermodynamicsElectrophoresis Polyacrylamide GelCarrier ProteinsPheromone binding proteinJournal of Biological Chemistry
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Bacteroides vulgatus protects against escherichia coli-induced colitis in gnotobiotic interleukin-2-deficient mice

2003

Abstract Background & Aims: The microflora plays a crucial role in inflammatory bowel diseases (IBDs). Specific pathogen-free (SPF), but not germ-free, interleukin (IL)-2-deficient (IL-2−/−) mice develop colitis. The colitogenicity of commensal bacteria was determined. Methods: Gnotobiotic IL-2−/− and IL-2+/+ mice were colonized with Escherichia coli mpk, Bacteroides vulgatus mpk, or both bacterial strains, or with E. coli strain Nissle 1917. DNA arrays were used to characterize E. coli mpk. Colitis was analyzed by histology and real-time reverse-transcription polymerase chain reaction (RT-PCR) for interferon (IFN)-γ, tumor necrosis factor (TNF)-α, IL-10, and CD14 messenger RNA (mRNA) expre…

MaleGene Expressionmedicine.disease_causeMicrobiologyFecesMiceInterferonEscherichia colimedicineAnimalsBacteroidesGerm-Free LifeColitisEscherichia coliBacteroidaceaeEscherichia coli InfectionsSpecific-pathogen-freeHepatologybiologyGastroenterologyInterleukinColitismedicine.diseasebiology.organism_classificationEnterobacteriaceaeMice Mutant StrainsSpecific Pathogen-Free OrganismsIntestinesMice Inbred C57BLInterleukin-2FemaleTumor necrosis factor alphamedicine.drugGastroenterology
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Echinostoma caproni: identification of enolase in excretory/secretory products, molecular cloning, and functional expression.

2007

In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, observed to be one of the most abundant proteins, was further characterized. The molecular cloning and in vitro expression in Escherichia coli of E. caproni enolase allowed us to determine that the protein contains 431 amino acids and a theoretical MW of 46272 Da. E. caproni enolase shows high homology to other trematode enolases. The recombinant protein binds specifically to human plasminogen in vitr…

MaleImmunologyEnolaseBlotting WesternMolecular Sequence DataMolecular cloningBiologymedicine.disease_causeGene Expression Regulation Enzymologiclaw.inventionlawCricetinaeEchinostomamedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularRats WistarEscherichia coliActinchemistry.chemical_classificationMesocricetusSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionPlasminogenGeneral MedicineMolecular biologyIn vitroRecombinant ProteinsAmino acidRatsInfectious DiseaseschemistryBiochemistryExcretory systemPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationRecombinant DNAParasitologyElectrophoresis Polyacrylamide GelSequence AlignmentExperimental parasitology
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Prevalence, genetic diversity of and factors associated with ESBL-producing Enterobacterales carriage in residents of French nursing homes

2019

Summary Objective To determine the prevalence and genotypic characteristics of extended-spectrum β-lactamase-producing Enterobacterales (ESBLE) and carbapenemase-producing Enterobacterales (CPE) in nursing homes (NHs) in a French region. Risk factors associated with their carriage were also investigated. Methods A point-prevalence survey was proposed from November 2017 to June 2018 to NHs in the study region. Volunteer residents were screened for ESBLE and CPE carriage. Escherichia coli and Klebsiella pneumoniae isolates were genotyped using multi-locus sequence typing, pulsed-field gel electrophoresis (PFGE) and phylogrouping (for E. coli alone). Collective and individual data were analyse…

MaleKlebsiella pneumoniaeEpidemiology030501 epidemiologyElderlyEpidemiologyGenotypePrevalenceMedicineEscherichia coli Infectionshealth care economics and organizationsAged 80 and over0303 health sciencesbiologyGeneral MedicineMiddle Aged3. Good healthKlebsiella pneumoniaeInfectious Diseases[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyFemaleFrance0305 other medical scienceMicrobiology (medical)medicine.medical_specialtyGenotypeNursing homesbeta-Lactamases03 medical and health sciencesBacterial ProteinsEnterobacteriaceaeInternal medicinePulsed-field gel electrophoresisEscherichia coliHumansTypingAgedGenetic diversity030306 microbiologybusiness.industryGenetic Variationbiochemical phenomena metabolism and nutritionbiology.organism_classificationKlebsiella InfectionsCross-Sectional StudiesCarriageESBLRisk factorsbusinessNursing homes
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CTX-M β-Lactamase-Producing Escherichia coli in French Hospitals: Prevalence, Molecular Epidemiology, and Risk Factors▿

2007

ABSTRACT In 2004, 65 CTX-M-producing Escherichia coli isolates were collected from infected patients in four French hospitals. The bla CTX-M-15 genes were predominant. Pulsed-field gel electrophoresis highlighted a clonal propagation of CTX-M-15-producing strains belonging to phylogenetic group B2, notably in the community. The main risk factors for acquiring these isolates were urinary tract infections or the presence of a urinary catheter in diabetic or renal failure patients.

MaleMESH : Escherichia coliMESH : PrevalenceEpidemiologyMESH : AgedMESH: beta-LactamasesMESH: Urinary Tract Infectionsmedicine.disease_causeMESH: Risk Factors[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseasesRisk FactorsGenotypePrevalenceMESH : Urinary Tract InfectionsMESH : FemaleMESH: PhylogenyEscherichia coli InfectionsPhylogenyGel electrophoresisMESH: Aged0303 health sciencesMolecular EpidemiologybiologyMESH: Escherichia coliMESH : beta-LactamasesMESH: HospitalsEnterobacteriaceaeMESH : Risk FactorsHospitals3. Good healthElectrophoresis Gel Pulsed-FieldMESH : Hospitals[ SDV.MHEP.MI ] Life Sciences [q-bio]/Human health and pathology/Infectious diseasesMESH: Electrophoresis Gel Pulsed-FieldMESH : Escherichia coli InfectionsUrinary Tract Infections[SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseasesFemaleFranceMicrobiology (medical)Urinary systemMESH : Malebeta-LactamasesMicrobiologyMESH : Epidemiology Molecular03 medical and health sciencesMESH: Epidemiology MolecularmedicineEscherichia coliHumansRisk factorMESH : FranceEscherichia coliMESH: Prevalence030304 developmental biologyMESH : Electrophoresis Gel Pulsed-FieldMESH: Escherichia coli InfectionsAgedMESH: HumansMolecular epidemiology030306 microbiologyMESH : HumansMESH : Phylogenybiology.organism_classificationMESH: MaleMESH: FranceMESH: FemaleBacteria
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