Search results for " Outer"

showing 10 items of 129 documents

Utilization of hemin and hemoglobin by Vibrio vulnificus biotype 2

1996

The eel pathogen Vibrio vulnificus biotype 2 is able to use hemoglobin (Hb) and hemin (Hm) to reverse iron limitation. In this stud, the adjuvant effect of both compounds on eel pathogenicity has been evaluated and confirmed. Further, we have studied the heme-iron acquisition mechanism displayed by this bacterium. Whole cells were capable of binding Hb and Hm, independently of (i) iron levels in growth medium and (ii) the presence of polysaccharide capsules on bacterial surface. The Hb- and Hm-binding capacity was retained by the outer membrane protein (OMP) fraction and was abolished after proteolytic digestion of OMP samples. Western blotting (immunoblotting) of denatured OMPs revealed th…

IronVibrio vulnificusApplied Microbiology and BiotechnologyMicrobiologyHemoglobinschemistry.chemical_compoundVibrionaceaeAnimalsHemeVibrioEelsVirulenceEcologybiologyProteolytic enzymesbacterial infections and mycosesbiology.organism_classificationVibriochemistryBiochemistryHeminbacteriaHemoglobinCarrier ProteinsBacterial outer membraneBacterial Outer Membrane ProteinsResearch ArticleFood ScienceBiotechnologyHeminApplied and Environmental Microbiology
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Regulatory O 2 tensions for the synthesis of fermentation products in Escherichia coli and relation to aerobic respiration

1997

In an oxystat, the synthesis of the fermentation products formate, acetate, ethanol, lactate, and succinate of Escherichia coli was studied as a function of the O2 tension (pO2) in the medium. The pO2 values that gave rise to half-maximal synthesis of the products (pO0. 5) were 0.2-0.4 mbar for ethanol, acetate, and succinate, and 1 mbar for formate. The pO0.5 for the expression of the adhE gene encoding alcohol dehydrogenase was approximately 0.8 mbar. Thus, the pO2 for the onset of fermentation was distinctly lower than that for anaerobic respiration (pO0.5/= 5 mbar), which was determined earlier. An essential role for quinol oxidase bd in microaerobic growth was demonstrated. A mutant de…

Iron-Sulfur ProteinsAnaerobic respirationFormatesCellular respirationSuccinic AcidAcetatesBiologymedicine.disease_causeColiphagesBiochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundBioreactorsBacterial ProteinsMultienzyme ComplexesEscherichia coliGeneticsmedicineFormateAnaerobiosisMolecular BiologyEscherichia coliMixed acid fermentationAlcohol dehydrogenaseNitratesEthanolEthanolEscherichia coli ProteinsAlcohol DehydrogenaseGene Expression Regulation BacterialGeneral MedicineAldehyde OxidoreductasesAerobiosisArtificial Gene FusionOxygenRepressor ProteinsLac OperonchemistryBiochemistryFermentationLactatesbiology.proteinFermentationOxidoreductasesBacterial Outer Membrane ProteinsArchives of Microbiology
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O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli

1996

With an oxystat, changes in the pattern of expression of FNR-dependent genes from Escherichia coli were studied as a function of the O2 tension (pO2) in the medium. Expression of all four tested genes was decreased by increasing O2. However, the pO2 values that gave rise to half-maximal repression (pO(0.5)) were dependent on the particular promoter and varied between 1 and 5 millibars (1 bar = 10(5) Pa). The pO(0.5) value for the ArcA-regulated succinate dehydrogenase genes was in the same range (pO(0.5) = 4.6 millibars). At these pO2 values, the cytoplasm can be calculated to be well supplied with O2 by diffusion. Therefore, intracellular O2 could provide the signal to FNR, suggesting that…

Iron-Sulfur ProteinsCellular respirationRepressorBiologymedicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsGenes RegulatorEscherichia colimedicineAnaerobiosisMolecular BiologyEscherichia coliRegulation of gene expressionchemistry.chemical_classificationEscherichia coli ProteinsSuccinate dehydrogenaseMembrane ProteinsGene Expression Regulation BacterialElectron transport chainAerobiosisOxygenRepressor ProteinsSuccinate DehydrogenaseEnzymeLac OperonchemistryBiochemistryGenes BacterialMutationbiology.proteinOxidation-ReductionProtein KinasesIntracellularBacterial Outer Membrane ProteinsSignal TransductionResearch ArticleJournal of Bacteriology
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Human kininogens interact with M protein, a bacterial surface protein and virulence determinant.

1995

Streptococcus pyogenes, the most significant streptococcal species in clinical medicine, expresses surface proteins with affinity for several human plasma proteins. Here we report that kininogens, the precursors to the vasoactive kinins, bind to the surface of S. pyogenes. M protein, a surface molecule and a major virulence factor-in these bacteria, occurs in > 80 different serotypes. Among 49 strains of S. pyogenes, all of different M serotypes, 41 bound radiolabelled kininogens, whereas 6 M protein-negative mutant strains showed no affinity. M protein of most serotypes bind fibrinogen, and among the 55 strains tested, binding of kininogens was closely correlated to fibrinogen bindi…

Kininogen bindingMyeloma proteinStreptococcus pyogenesM1 proteinMolecular Sequence DataEnzyme-Linked Immunosorbent Assaymedicine.disease_causeBiochemistryPeptide MappingAntibodiesBacterial ProteinsmedicineHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenAntigens BacterialBinding SitesbiologyVirulenceKininogensFibrinogen bindingFibrinogenCell BiologyLow-molecular-weight kininogenMolecular biologyStreptococcus pyogenesbiology.proteinCarrier Proteinscirculatory and respiratory physiologyResearch ArticleBacterial Outer Membrane ProteinsProtein Binding
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Dual Labeling of Lipopolysaccharides for SPECT-CT Imaging and Fluorescence Microscopy.

2013

International audience; : Lipopolysaccharides (LPS) or endotoxins are amphipathic, pro-inflammatory components of the outer membrane of Gram-negative bacteria. In the host, LPS can trigger a systemic inflammatory response syndrome. To bring insight into in vivo tissue distribution and cellular uptake of LPS, dual labeling was performed with a bimodal molecular probe designed for fluorescence and nuclear imaging. LPS were labeled with DOTA-Bodipy-NCS, and pro-inflammatory properties were controlled after each labeling step. LPS were then radiolabeled with (111)In and subsequently injected intravenously into wild-type, C57B16 mice, and their in vivo behavior was followed by single photon emis…

LipopolysaccharidesBiodistribution[CHIM.THER]Chemical Sciences/Medicinal Chemistry[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology010402 general chemistry01 natural sciencesBiochemistryLipopolysaccharide transport03 medical and health sciencesMiceIn vivoCoordination ComplexesFluorescence microscope[INFO.INFO-IM]Computer Science [cs]/Medical ImagingAnimals[CHIM.COOR]Chemical Sciences/Coordination chemistryTissue Distribution030304 developmental biologyFluorescent DyesTomography Emission-Computed Single-Photon0303 health sciencesMolecular Structure[ INFO.INFO-IM ] Computer Science [cs]/Medical ImagingChemistryIndium Radioisotopes[ CHIM.COOR ] Chemical Sciences/Coordination chemistry[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology[ CHIM.THER ] Chemical Sciences/Medicinal ChemistryGeneral MedicineFluorescence0104 chemical sciencesMice Inbred C57BLMicroscopy FluorescenceIsotope LabelingBiophysicsMolecular Medicinelipids (amino acids peptides and proteins)Bacterial outer membraneMolecular probe[CHIM.RADIO]Chemical Sciences/Radiochemistry[ CHIM.RADIO ] Chemical Sciences/RadiochemistryEx vivo
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Vibrio vulnificus biotype 2 serovar E gne but not galE is essential for lipopolysaccharide biosynthesis and virulence

2008

ABSTRACT This work aimed to establish the role of gne (encoding UDP-GalNAc 4-epimerase activity) and galE (encoding UDP-Gal-4-epimerase activity) in the biosynthesis of surface polysaccharides, as well as in the virulence for eels and humans of the zoonotic serovar of Vibrio vulnificus biotype 2, serovar E. DNA sequence data revealed that gne and galE are quite homologous within this species (≥90% homology). Mutation in gne of strain CECT4999 increased the surface hydrophobicity, produced deep alterations in the outer membrane architecture, and resulted in noticeable increases in the sensitivity to microcidal peptides (MP), to eel and human sera, and to phagocytosis/opsonophagocytosis. Furt…

LipopolysaccharidesLipopolysaccharidePhagocytosisMolecular Sequence DataImmunologyMutantVirulenceVibrio vulnificusMicrobiologyMicrobiologyMiceUDPglucose 4-Epimerasechemistry.chemical_compoundBacterial ProteinsPhagocytosisVibrionaceaeAnimalsCloning MolecularVibrio vulnificusPhagocytesEelsBase SequenceVirulencebiologyChemotaxisTransferrinGene Expression Regulation Bacterialbiology.organism_classificationMolecular PathogenesisComplementationcarbohydrates (lipids)Infectious DiseaseschemistryBiofilmsMutationBacteris patògensParasitologyCarbohydrate EpimerasesBacterial outer membraneAntimicrobial Cationic Peptides
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O-Serogrouping and surface components ofAeromonas hydrophilaandAeromonas jandaeipathogenic for eels

1994

The relationship between virulence, O-serogroup, and some cell-surface features (self-pelleting [SP] and precipitation after boiling [PAB], profile of lipopolysaccharides [LPSs] and outer membrane proteins [OMPs]) was investigated in strains of the pathogenic species Aeromonas hydrophila and A. jandaei isolated from eels. Virulent strains of A. hydrophila reacted mostly with O:19 antiserum, and those of A. jandaei reacted with O:4, O:11, O:15 and O:29 antisera (Guinée and Jansen system). Regarding the PAB and LPS profiles two groups could be distinguished; (i) five PAB+ strains of serotype O:19 that possessed a homogeneous O polysaccharide side chain and (ii) thirteen PAB- strains antigenic…

LipopolysaccharidesSerotypeVirulenceBiologyMicrobiologyMicrobiologyVibrionaceaeGeneticsAnimalsSerotypingMolecular BiologyAntiserumEelsVirulenceCell MembranePolysaccharides BacterialO Antigensbiology.organism_classificationAntibodies BacterialAeromonas hydrophilaAeromonas hydrophilaPhenotypeAeromonasAeromonas jandaeiAeromonasBacteriaBacterial Outer Membrane ProteinsFEMS Microbiology Letters
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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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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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ApoB100,LDLR-/- mice exhibit reduced electroretinographic response and cholesteryl esters deposits in the retina

2008

International audience; PURPOSE. To evaluate the retinal phenotype of 7- and 14-month-old apoB100,LDLR–/– mice, a relevant animal model of lipid metabolism dysfunction. METHODS. Single-flash electroretinograms were obtained from 7- and 14-month-old apoB100,LDLR–/– and control mice fed a standard diet under both scotopic and photopic conditions. Visual cycle retinoids were analyzed in eyes from dark-adapted mice. Retinal and choroidal vascularization was evaluated with scanning laser ophthalmoscopy. Fatty acids were analyzed in the retina. Esterified and free cholesterol was detected in eye cryosections. RESULTS. Scotopic and photopic b-wave amplitudes were significantly reduced in apoB100,L…

MaleHUMAN BRUCHS MEMBRANEgenetic structuresHIGH-FAT DIETLipid Metabolism DisordersBasement MembraneAGE-RELATED MACULOPATHYchemistry.chemical_compoundMice0302 clinical medicine[SDV.IDA]Life Sciences [q-bio]/Food engineeringFluorescein AngiographyPigment Epithelium of EyeTRANSGENIC MICE0303 health sciencesmedicine.diagnostic_testROD OUTER SEGMENTSmedicine.anatomical_structureBiochemistryHUMAN APOLIPOPROTEIN-BApolipoprotein B-100Femalelipids (amino acids peptides and proteins)Cholesterol EstersPhotopic visionVisual phototransductionmedicine.medical_specialtyDark AdaptationMice TransgenicBiologyRetinaRECEPTOR-NEGATIVE MICE03 medical and health sciencesRetinoidsRetinal DiseasesBASAL DEPOSITSInternal medicinemedicineElectroretinographyAnimals[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringFilipinHUMAN ATHEROSCLEROTIC LESIONS030304 developmental biologyRetinaRetinal pigment epitheliumRetinalMacular degenerationmedicine.diseaseMACULAR DEGENERATIONeye diseasesMice Inbred C57BLOphthalmoscopyEndocrinologychemistryReceptors LDLLDL receptor030221 ophthalmology & optometrysense organsPhotic StimulationElectroretinography
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