Search results for "bacterial"

showing 10 items of 3246 documents

[Legionella spp. contamination in indoor air: preliminary results of an Italian multicenter study].

2014

Obiettivo. Rilevare la presenza di Legionella spp. nell’aria attraverso un protocollo standardizzato, a fianco dei tradizionali metodi impiegati per la rete idrica. Disegno. In dieci strutture sanitarie è stato selezionato un bagno, la cui acqua presentava una contaminazione da Legionella >1.000 unità formanti colonie (ufc)/litro. La contaminazione dell’aria è stata valutata tramite campionamento attivo (Surface Air System, SAS) e passivo, impiegando piastre di sedimentazione per la valutazione dell’Indice Microbico Aria (Index of Microbial Air, IMA). I campionamenti sono stati effettuati per 8 ore consecutive, a circa 1 m dal pavimento e a 50 cm dal rubinetto. Con il campionamento attivo, …

Air MicrobiologyLegionellaLegionella indoor ariaindoor airSettore MED/42 - Igiene Generale E ApplicataWaste Disposal FluidcontaminationAir PollutionHumansIndoorToilet FacilitiesCross InfectionLegionellosislegionella spp; contamination; indoor airLegionella aria acqua SAS IMAWaste Disposalbacterial infections and mycosesariaHospitalsrespiratory tract diseasesBacterial Typing TechniquesItalyAir Pollution IndoorBacterial Typing Techniques; Cross Infection; Environmental Monitoring; Hospitals; Humans; Italy; Legionella; Legionellosis; Toilet Facilities; Waste Disposal Fluid; Water Microbiology; Air Microbiology; Air Pollution Indoorlegionella sppbacteriaFluidWater MicrobiologyEnvironmental MonitoringEpidemiologia e prevenzione
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Preferential localization of Lactococcus lactis cells entrapped in a caseinate/alginate phase separated system.

2013

International audience; This study aimed to entrap bioprotective lactic acid bacteria in a sodium caseinate/sodium alginate aqueous two-phase system. Phase diagram at pH = 7 showed that sodium alginate and sodium caseinate were not miscible when their concentrations exceeded 1% (w/w) and 6% (w/w), respectively. The stability of the caseinate/alginate two-phase system was also checked at pH values of 6.0 and 5.5. Lactococcus lactis subsp. lactis LAB3 cells were added in a 4% (w/w) caseinate/1.5% (w/w) alginate two-phase system at pH = 7. Fluorescence microscopy allowed to observe that the caseinate-rich phase formed droplets dispersed in a continuous alginate-rich phase. The distribution of …

Alginates02 engineering and technologyCell SeparationHydrophobic effectchemistry.chemical_compound0404 agricultural biotechnologyColloid and Surface ChemistryGlucuronic AcidPhase (matter)Fluorescence microscope[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPhysical and Theoretical ChemistryAqueous solutionChromatographybiologyHexuronic AcidsLactococcus lactisAqueous two-phase systemCaseins04 agricultural and veterinary sciencesSurfaces and InterfacesGeneral MedicineHydrogen-Ion Concentration021001 nanoscience & nanotechnologybiology.organism_classification040401 food scienceLactic acidPhase diagramLactococcus lactisSodium caseinateBiochemistrychemistryAqueous two-phase system0210 nano-technologySodium alginateBacteriaBacterial cells entrapmentBiotechnologyColloids and surfaces. B, Biointerfaces
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Structure-Function Relationship of Substituted Bromomethylcoumarins in Nucleoside Specificity of RNA Alkylation

2013

Selective alkylation of RNA nucleotides is an important field of RNA biochemistry, e.g. in applications of fluorescent labeling or in structural probing experiments, yet detailed structure-function studies of labeling agents are rare. Here, bromomethylcoumarins as reactive compounds for fluorescent labeling of RNA are developed as an attractive scaffold on which electronic properties can be modulated by varying the substituents. Six different 4-bromomethyl-coumarins of various substitution patterns were tested for nucleotide specificity of RNA alkylation using tRNA from Escherichia coli as substrate. Using semi-quantitative LC-MS/MS analysis, reactions at mildly acidic and slightly alkaline…

AlkylationStaining and LabelingScienceQRNucleosidesRNA BacterialStructure-Activity RelationshipRNA TransferCoumarinsEscherichia coliMedicine500 Natural sciences and mathematics500 NaturwissenschaftenResearch ArticleFluorescent DyesPLoS ONE
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Effective treatment of allergic airway inflammation with Helicobacter pylori immunomodulators requires BATF3-dependent dendritic cells and IL-10

2014

The prevalence of allergic asthma and other atopic diseases has reached epidemic proportions in large parts of the developed world. The gradual loss of the human indigenous microbiota has been held responsible for this trend. The bacterial pathogen Helicobacter pylori is a constituent of the normal gastric microbiota whose presence has been inversely linked to allergy and asthma in humans and experimental models. Here we show that oral or i.p. tolerization with H. pylori extract prevents the airway hyperresponsiveness, bronchoalveolar eosinophilia, pulmonary inflammation, and Th2 cytokine production that are hallmarks of allergen-induced asthma in mice. Asthma protection is not conferred by…

Allergybacterial persistence determinantsT-Lymphocytes Regulatorybacterial immunomodulationImmune toleranceMiceBacterial ProteinsImmune TolerancemedicineAnimalsHumansImmunologic FactorsEosinophiliaAsthmaMice KnockoutAntigens Bacterial1000 MultidisciplinaryMultidisciplinaryHelicobacter pyloribiologyallergy and asthma prevention10061 Institute of Molecular Cancer ResearchInterleukin-18tolerogenic dendritic cellsDendritic Cellsgamma-GlutamyltransferaseDendritic cellBiological SciencesAllergensHelicobacter pyloribacterial infections and mycosesmedicine.diseasebiology.organism_classificationAsthmaInterleukin-10respiratory tract diseases3. Good healthMice Inbred C57BLRepressor ProteinsDisease Models AnimalInterleukin 10Basic-Leucine Zipper Transcription FactorsImmunology570 Life sciences; biologyInterleukin 18medicine.symptom
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Paramagnetic NMR investigations of Co(II) and Ni(II) amicyanin.

1999

The paramagnetic 1H NMR spectra of the Co(II) and Ni(II) substituted forms of the type 1 blue copper protein (cupredoxin) amicyanin have been assigned. This is the first such analysis of a cupredoxin, which has a distorted tetrahedral active site with the ligands provided by two histidines, a cysteine and a methionine. The isotropic shifts of the resonances in these spectra are compared with those of Co(II) and Ni(II) azurin. A number of interesting similarities and differences are found. The coordination of the metal by the two equatorial histidine ligands is very similar in both proteins. The interaction between the introduced metal and the thiolate sulfur of the equatorial cysteine ligan…

AmicyaninMagnetic Resonance SpectroscopyCopper proteinPhotochemistryLigandsBiochemistryInorganic ChemistryMethionineBacterial ProteinsAzurinNickelHistidineHistidineBinding SitesbiologyLigandChemistryActive siteCobaltCrystallographybiology.proteinProton NMRSpectrophotometry UltravioletAzurinCopperCysteineJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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CyaC, a redox-regulated adenylate cyclase of Sinorhizobium meliloti with a quinone responsive diheme-B membrane anchor domain.

2019

The nucleotide cyclase CyaC of Sinorhizobium meliloti is a member of class III adenylate cyclases (AC), a diverse group present in all forms of life. CyaC is membrane-integral by a hexahelical membrane domain (6TM) with the basic topology of mammalian ACs. The 6TM domain of CyaC contains a tetra-histidine signature that is universally present in the membrane anchors of bacterial diheme-B succinate-quinone oxidoreductases. Heterologous expression of cyaC imparted activity for cAMP formation from ATP to Escherichia coli, whereas guanylate cyclase activity was not detectable. Detergent solubilized and purified CyaC was a diheme-B protein and carried a binuclear iron-sulfur cluster. Single poin…

Amino Acid Transport SystemsAdenylate kinasemedicine.disease_causeMicrobiologyCyclase03 medical and health sciencesmedicineBenzoquinonesNucleotideHistidineAmino Acid SequenceMolecular BiologyEscherichia coliHistidine030304 developmental biologychemistry.chemical_classification0303 health sciencesSinorhizobium melilotibiology030306 microbiologyEscherichia coli ProteinsGuanylate cyclase activityQuinonesMembrane Proteinsbiology.organism_classificationchemistryBiochemistryGenes BacterialHeterologous expressionOxidation-ReductionAdenylyl CyclasesSinorhizobium melilotiMolecular microbiology
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Synthesis of Peroxyapatite by Hydrothermal Processing

2014

Peroxide ions in apatite provides an additional resource for imparting an antibacterial capability in apatite. A hydrothermal process has been developed for including peroxide ions into the apatite lattice. Three oxygen generation compounds, hydrogen peroxide, ammonium persulphate and paracetic acid were investigated for peroxyapatite generation. Hydrogen peroxide provides the highest peroxide containing apatite. Both the oxygen generation and the apatite lattice formation represented the two critical factors for producing peroxyapatite. Unlike with high temperature processing, the cooling rate did not influence the retained peroxide content. This new process provides a building block for i…

Ammonium persulphateMechanical EngineeringInorganic chemistrychemistry.chemical_elementhydrogen peroxidePeroxideOxygenApatiteHydrothermal circulationIonantibacterialchemistry.chemical_compoundCooling ratechemistryhydrothermal processingMechanics of Materialsvisual_artvisual_art.visual_art_mediumGeneral Materials ScienceHydrogen peroxideperoxyapatiteKey Engineering Materials
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Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications

1997

In Escherichia coli the expression of the nuo genes encoding the proton pumping NADH dehydrogenase I is stimulated by the presence of fumarate during anaerobic respiration. The regulatory sites required for the induction by fumarate, nitrate and O2 are located at positions around –309, –277, and downstream of –231 bp, respectively, relative to the transcriptional-start site. The fumarate regulator has to be different from the O2 and nitrate regulators ArcA and NarL. For growth by fumarate respiration, the presence of NADH dehydrogenase I was essential, in contrast to aerobic or nitrate respiration which used preferentially NADH dehydrogenase II. The electron transport from NADH to fumarate …

Anaerobic respirationAcetatesmedicine.disease_causeBiochemistryElectron TransportFumaratesEscherichia colimedicineDimethyl SulfoxideNADH NADPH OxidoreductasesAnaerobiosisEscherichia colichemistry.chemical_classificationElectron Transport Complex IEthanolbiologyNADH dehydrogenaseGene Expression Regulation BacterialProton PumpsElectron acceptorFumarate reductaseNADElectron transport chainGlycerol-3-phosphate dehydrogenaseBiochemistrychemistryElectron Transport Complex Ibiology.proteinEnergy MetabolismEuropean Journal of Biochemistry
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Transport of C(4)-dicarboxylates in Wolinella succinogenes.

2000

ABSTRACT C 4 -dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes , since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C 4 -dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10 3 . The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the prese…

Anaerobic respirationAntiporterPhysiology and MetabolismMutantMalatesBiologymedicine.disease_causeMicrobiologyCell membraneElectron TransportOxygen ConsumptionBacterial ProteinsFumaratesRespirationmedicineDicarboxylic AcidsAnaerobiosisMolecular BiologyEscherichia coliDicarboxylic Acid TransportersAspartic AcidNitratesEscherichia coli ProteinsCell MembraneSodiumMembrane ProteinsBiological TransportSuccinatesFumarate reductaseElectron transport chainWolinellamedicine.anatomical_structureBiochemistryMutagenesisCarrier ProteinsGene DeletionJournal of bacteriology
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Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors

1997

AbstractThe electron-transport chains of Escherichia coli are composed of many different dehydrogenases and terminal reductases (or oxidases) which are linked by quinones (ubiquinone, menaquinone and demethylmenaquinone). Quinol:cytochrome c oxido-reductase (`bc1 complex') is not present. For various electron acceptors (O2, nitrate) and donors (formate, H2, NADH, glycerol-3-P) isoenzymes are present. The enzymes show great variability in membrane topology and energy conservation. Energy is conserved by conformational proton pumps, or by arrangement of substrate sites on opposite sides of the membrane resulting in charge separation. Depending on the enzymes and isoenzymes used, the H+/e− rat…

Anaerobic respirationTranscription GeneticCellular respirationFNRBiophysicsBiochemistryElectron TransportOxygen sensorOxygen ConsumptionBacterial Proteins(Escherichia coli)Escherichia coliProtein phosphorylationAnaerobiosischemistry.chemical_classificationbiologyCytochrome cQuinonesArcAGene Expression Regulation BacterialCell BiologyElectron acceptorElectron transport chainAerobiosisAerobic electron transportResponse regulatorAnaerobic electron transportBiochemistrychemistrybiology.proteinCarrier ProteinsEnergy MetabolismOxidoreductasesFlux (metabolism)RegulationBiochimica et Biophysica Acta (BBA) - Bioenergetics
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