Search results for "bacterial protein"

showing 10 items of 616 documents

Role of the virulence plasmid pR99 and the metalloprotease Vvp in resistance of Vibrio vulnificus serovar E to eel innate immunity

2007

Vibrio vulnificus biotype 2 serovar E (VSE) is a bacterial pathogen that produces a haemorrhagic septicaemia called vibriosis in eels. Its ability to grow in blood is conferred by a recently described virulence plasmid [Lee CT, Amaro C, Wu KM, Valiente E, Chang YF, Tsai SF, et al. A common virulence plasmid in biotype 2 Vibrio vulnificus and its dissemination aided by a conjugal plasmid. Journal of Bacteriology, submitted for publication.]. In this study, we analyzed the role of this plasmid together with the role played by the metalloprotease (Vvp) in the interaction between bacteria and eel innate immunity. To this end, we compared and statistically analyzed the differences in resistance …

Antimicrobial peptidesVirulenceMicrobial Sensitivity TestsVibrio vulnificusAquatic ScienceMicrobiologyPlasmidAnti-Infective AgentsBacterial ProteinsPhagocytosisBacteriologyAnimalsEnvironmental ChemistryImmunity MucosalVibrio vulnificusPathogenAntigens BacterialPhagocytesInnate immune systembiologyComplement Fixation TestsTransferrinMetalloendopeptidasesGeneral MedicineAnguillabiology.organism_classificationAntibodies BacterialVirologyImmunity InnateAntigens SurfaceMutationAlternative complement pathwayMuramidaseAntimicrobial Cationic PeptidesPlasmidsFish & Shellfish Immunology
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Oxidative stress protection by manganese complexes of tail-tied aza-scorpiand ligands.

2015

The Mn2+ coordination chemistry of double scorpiand ligands in which two polyazacyclophane macrocycles have been connected by pyridine, phenanthroline and bipyridine spacers has been studied by potentiometry, paramagnetic NMR and electrochemistry. All ligands show high stability with Mn2+ and the complexes were formed in a wide pH range. DFT calculations support the structures and coordination geometries derived from the study. A remarkable antioxidant activity was evidenced for these systems by the McCord-Fridovich assay and in Escherichiacoli sodAsodB deficient bacterial cells. The three systems were tested as anti-inflammatory drugs in human macrophages measuring the accumulation of cyto…

AntioxidantStereochemistrymedicine.medical_treatmentPhenanthrolineInorganic chemistrychemistry.chemical_elementManganese010402 general chemistryElectrochemistry01 natural sciencesBiochemistryAntioxidantsCoordination complexInorganic ChemistrySuperoxide dismutasechemistry.chemical_compoundBipyridineBacterial ProteinsCoordination ComplexesCell Line TumorPyridinemedicineEscherichia coliHumanschemistry.chemical_classificationManganesebiology010405 organic chemistryChemistrySuperoxide DismutaseMacrophagesAnti-Inflammatory Agents Non-Steroidal0104 chemical sciencesOxidative Stressbiology.proteinJournal of inorganic biochemistry
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DctA- and Dcu-independent transport of succinate in Escherichia coli : contribution of diffusion and of alternative carriers

2001

Quintuple mutants of Escherichia coli deficient in the C4-dicarboxylate carriers of aerobic and anaerobic metabolism (DctA, DcuA, DcuB, DcuC, and the DcuC homolog DcuD, or the citrate/succinate antiporter CitT) showed only poor growth on succinate (or other C4-dicarboxylates) under oxic conditions. At acidic pH (pH 6) the mutants regained aerobic growth on succinate, but not on fumarate. Succinate uptake by the mutants could not be saturated at physiological succinate concentrations (≤5 mM), in contrast to the wild-type, which had a K m for succinate of 50 µM and a V max of 35 U/g dry weight at pH 6. At high substrate concentrations, the mutants showed transport activities (32 U/g dry weigh…

AntiporterMutantSuccinic AcidBiologymedicine.disease_causeBiochemistryMicrobiologyBacterial ProteinsFumaratesNitrilesEscherichia coliGeneticsmedicineMolecular BiologyEscherichia coliDicarboxylic Acid TransportersUncoupling AgentsEscherichia coli ProteinsBiological TransportGeneral MedicineMetabolismHydrogen-Ion ConcentrationFumarate reductasebiology.organism_classificationEnterobacteriaceaeBiochemistryMutationFermentationEffluxCarrier ProteinsArchives of Microbiology
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Pathogenic Aeromonas hydrophila Serogroup O:14 and O:81 Strains with an S Layer

2004

ABSTRACT Five autoagglutinating Aeromonas hydrophila isolates recovered from eels and humans were assigned to serogroups O:14 and O:81 of the Sakazaki and Shimada (National Institutes of Health) scheme. They had the following properties in common: positive precipitation after boiling, moderate surface hydrophobicity (salt-aggregation-test value around 1.2), pathogenicity for fish and mice (50% lethal dose, 10 4.61 to 10 7.11 ), lipopolysaccharides that contained O-polysaccharide chains of homogeneous chain length, and an external S layer peripheral to the cell wall observed by electron microscopy. A strong cross-reactivity was detected by immunoblotting between the homogeneous O-polysacchar…

Applied Microbiology and BiotechnologyMicrobiologyMiceBacterial ProteinsSpecies SpecificityVibrionaceaeEnvironmental MicrobiologyAnimalsHumansSerotypingEelsVirulenceEcologybiologyStrain (chemistry)EcologyStructural geneMembrane Proteinsbiology.organism_classificationAeromonas hydrophilaMolecular WeightMicroscopy ElectronAeromonas salmonicidaAeromonas hydrophilaAeromonasGenes BacterialS-layerBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
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The Low-Affinity ATP Binding Site of the Escherichia coli SecA Dimer Is Localized at the Subunit Interface

1997

The homodimeric SecA protein is the ATP-dependent force generator in the Escherichia coli precursor protein translocation cascade. SecA contains two essential nucleotide binding sites (NBSs), i.e., NBS1 and NBS2 that hind ATP with high and low affinity, respectively. The photoactivatable bifunctional cross-linking agent 3'-arylazido-8-azidoadenosine 5'-triphosphate (diN(3)ATP) was used to investigate the spatial arrangement of the nucleotide binding sites of SecA, DiN(3)ATP is an authentic ATP analogue as it supports SecA-dependent precursor protein translocation and translocation ATPase, UV-induced photo-cross-linking of the diN(3)ATP-bound SecA results in the formation of stable dimeric s…

AzidesUltraviolet RaysProtein subunitATPaseDimerMutantPhotoaffinity LabelsBiologymedicine.disease_causeESSENTIAL COMPONENTenvironment and public healthBiochemistryBACILLUS-SUBTILISchemistry.chemical_compoundAdenosine TriphosphateBacterial ProteinsPROTON MOTIVE FORCEEscherichia colimedicinePRECURSOR PROTEIN TRANSLOCATIONNucleotideBinding siteEscherichia coliAdenosine Triphosphataseschemistry.chemical_classificationBinding SitesSecA ProteinsNucleotidesChemiosmosisEscherichia coli ProteinsMembrane Transport ProteinsPHOTOAFFINITY CROSS-LINKINGCross-Linking ReagentschemistryBiochemistryMEMBRANE-VESICLES REQUIRESPLASMA-MEMBRANE3'-ARYLAZIDO-BETA-ALANYL-8-AZIDO ATPCYTOPLASMIC MEMBRANEbiology.proteinPREPROTEIN TRANSLOCASEbacteriaDimerizationSEC Translocation ChannelsBiochemistry
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Disentangling the rhizosphere effect on nitrate reducers and denitrifiers: insight into the role of root exudates.

2008

International audience; To determine to which extent root-derived carbon contributes to the effects of plants on nitrate reducers and denitrifiers, four solutions containing different proportions of sugar, organic acids and amino acids mimicking maize root exudates were added daily to soil microcosms at a concentration of 150 μg C g−1 of soil. Water-amended soils were used as controls. After 1 month, the size and structure of the nitrate reducer and denitrifier communities were analysed using the narG and napA, and the nirK, nirS and nosZ genes as molecular markers respectively. Addition of artificial root exudates (ARE) did not strongly affect the structure or the density of nitrate reduce…

BACTERIAL COMMUNITY STRUCTURE REAL-TIME PCRDNA BacterialDenitrificationMolecular Sequence DataDIVERSITYBiologyGENETIC-STRUCTURENIRKNitrate reductaseMicrobiologyPlant RootsZea mays03 medical and health scienceschemistry.chemical_compoundNitrateBacterial ProteinsBotanyPLANTSSugarEcology Evolution Behavior and SystematicsNitritesSoil Microbiology030304 developmental biology2. Zero hunger0303 health sciencesRhizosphereNitratesBacteria04 agricultural and veterinary sciencesBiodiversitySequence Analysis DNA6. Clean waterCarbonSOIL[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitologychemistry13. Climate actionEnvironmental chemistrySoil water040103 agronomy & agriculture0401 agriculture forestry and fisheriesComposition (visual arts)MicrocosmOxidoreductasesOxidation-ReductionMAIZENOSZ GENESEnvironmental microbiology
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The Agr communication system provides a benefit to the populations of Listeria monocytogenes in soil

2014

International audience; In this study, we investigated whether the Agr communication system of the pathogenic bacterium Listeria monocytogenes was involved in adaptation and competitiveness in soil. Alteration of the ability to communicate, either by deletion of the gene coding the response regulator AgrA (response-negative mutant) or the signal pro-peptide AgrD (signal-negative mutant), did not affect population dynamics in soil that had been sterilized but survival was altered in biotic soil suggesting that the Agr system of L. monocytogenes was involved to face the complex soil biotic environment. This was confirmed by a set of co-incubation experiments. The fitness of the response-negat…

Bacillus-subtilisMutantlcsh:QR1-502Genetic Fitnessmicrobial ecologymedicine.disease_causelcsh:MicrobiologyQuorum-sensing systemsOriginal Research ArticlePseudomonas-aeruginosaSoil Microbiology2. Zero hunger0303 health sciencesMutationeducation.field_of_studycompetitivenessMicrobiology and Parasitologycell communicationMicrobiologie et ParasitologiefitnessAgricultural sciences[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyInfectious DiseasesSoil microbiologyMicrobiology (medical)PopulationImmunologyLactobacillus-plantarum[SDV.SA.SDS]Life Sciences [q-bio]/Agricultural sciences/Soil studyBiologyMicrobiologyMicrobiologysoil03 medical and health sciences[ SDV.SA.AGRO ] Life Sciences [q-bio]/Agricultural sciences/AgronomyBacterial ProteinsListeria monocytogenesmedicineAgr system;cell communication;competitiveness;fitness;Listeria monocytogenes;soil;biotic interaction;quorum-sensing systems;expression;farm environment;dairy farm;bacterial-populations;pseudomonas-aeruginosa;microbial world;lactobacillus-plantarum;staphylococcus-aureus;bacillus-subtilisStaphylococcus-aureuseducationGene030304 developmental biology[ SDV ] Life Sciences [q-bio]Bacterial-populations030306 microbiologybiotic interactionFarm environmentListeria monocytogenesResponse regulatorMutationDairy farmGenetic Fitnessmicrobial worldSciences agricolesAgr system
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Integrative Model for Binding of Bacillus thuringiensis Toxins in Susceptible and Resistant Larvae of the Diamondback Moth (Plutella xylostella)

1999

ABSTRACT Insecticidal crystal proteins from Bacillus thuringiensis in sprays and transgenic crops are extremely useful for environmentally sound pest management, but their long-term efficacy is threatened by evolution of resistance by target pests. The diamondback moth ( Plutella xylostella ) is the first insect to evolve resistance to B. thuringiensis in open-field populations. The only known mechanism of resistance to B. thuringiensis in the diamondback moth is reduced binding of toxin to midgut binding sites. In the present work we analyzed competitive binding of B. thuringiensis toxins Cry1Aa, Cry1Ab, Cry1Ac, and Cry1F to brush border membrane vesicles from larval midguts in a susceptib…

Bacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsApplied Microbiology and BiotechnologyBinding CompetitiveModels BiologicalHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalGeneticsBacillaceaeDiamondback mothBinding SitesEcologybiologyBacillus thuringiensis ToxinsParasporal bodyfungiPlutellafood and beveragesbiology.organism_classificationEndotoxinsCry1AcLarvaFood ScienceBiotechnology
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Production and characterization of Bacillus thuringiensis Cry1Ac-resistant cotton bollworm Helicoverpa zea (Boddie).

2007

ABSTRACT Laboratory-selected Bacillus thuringiensis -resistant colonies are important tools for elucidating B. thuringiensis resistance mechanisms. However, cotton bollworm, Helicoverpa zea , a target pest of transgenic corn and cotton expressing B. thuringiensis Cry1Ac (Bt corn and cotton), has proven difficult to select for stable resistance. Two populations of H. zea (AR and MR), resistant to the B. thuringiensis protein found in all commercial Bt cotton varieties (Cry1Ac), were established by selection with Cry1Ac activated toxin (AR) or MVP II (MR). Cry1Ac toxin reflects the form ingested by H. zea when feeding on Bt cotton, whereas MVP II is a Cry1Ac formulation used for resistance se…

Bacterial ToxinsBacillus thuringiensisMothsGossypiumApplied Microbiology and BiotechnologyCypermethrinInsecticide Resistancechemistry.chemical_compoundHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsPest Control BiologicalGossypiumGenetically modified maizeEcologybiologyBacillus thuringiensis Toxinsfungifood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticulturechemistryAgronomyCry1AcBt cottonHelicoverpa zeaPEST analysisFood ScienceBiotechnologyProtein BindingApplied and environmental microbiology
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Comparison of Different Methodologies for Binding Assays of Bacillus thuringiensis Toxins to Membrane Vesicles from Insect Midguts

2002

Bacterial ToxinsBacillus thuringiensisMothsSpodopteraHemolysin ProteinsCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanymedicineAnimalsEcology Evolution Behavior and SystematicsBacillaceaeBacillus thuringiensis ToxinsbiologyVesicleCell MembraneMidgutbiology.organism_classificationBacillalesEndotoxinsmedicine.anatomical_structureBiochemistryDigestive SystemBacteriaJournal of Invertebrate Pathology
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