Search results for "(Escherichia coli)"

showing 10 items of 689 documents

Paplašināta spektra β-laktamāzes kodējošo gēnu noteikšana Escherichia coli kultūrās, kas izolētas no mājas cūkām

2017

Darba mērķis bija izpētīt Pārtikas drošības, dzīvnieku veselības un vides zinātniskajā institūtā „BIOR” izolētas Escherichia coli kultūras, nosakot TEM, OXA, SHV, CTX-M I, CTX-M II, CTX-M IV, CMY II un DHA tipa β-laktamāzes gēnu klātbūtni baktēriju kultūru paraugos. Bakalaura darbs izstrādāts 2017. gadā zinātniskā institūta “BIOR” Dzīvnieku slimību diagnostikas laboratorijas Mikrobioloģijas nodaļā un Molekulārās bioloģijas nodaļā. Pētāmie paraugi (Escherichia coli kultūras) bija iegūti no mājas cūku (Sus scrofa domestica) aklo zarnu paraugiem 2016. un 2017. gada VPP “AgroBioRes” ietvaros. Kopā tika analizēti 68 Escherichia coli kultūru paraugi no dažādām saimniecībām. β-lactamāzeskodējošo g…

Sus scrofa domesticaantibiotic resistanceEscherichia coliBioloģijaextended spectrum β-lactamases
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Modular organization in the reductive evolution of protein-protein interaction networks

2006

Analysis of the reduction in genome size of Buchnera aphidicola from its common ancestor E. coli shows that the organization of networks into modules is the property that seems to be directly related with the evolutionary process of genome reduction.

Systems biologyComplex systemComputational biologyBiologyGenomeProtein protein interaction networkProtein–protein interactionBuchneraInteraction networkProtein Interaction MappingEscherichia coliAnimalsHumansDatabases ProteinGeneticsbusiness.industrySystems BiologyResearchbiochemical phenomena metabolism and nutritionModular designbiology.organism_classificationBiological EvolutionProtein Structure TertiaryStructural Homology ProteinMultiprotein ComplexesBuchnerabusinessAlgorithmsGenome BacterialGenome Biology
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Unexpected Modulation of Recall B and T Cell Responses after Immunization with Rotavirus-like Particles in the Presence of LT-R192G

2010

LT-R192G, a mutant of the thermolabile enterotoxin of E. coli, is a potent adjuvant of immunization. Immune responses are generally analyzed at the end of protocols including at least 2 administrations, but rarely after a prime. To investigate this point, we compared B and T cell responses in mice after one and two intrarectal immunizations with 2/6 rotavirus-like particles (2/6-VLP) and LT-R192G. After a boost, we found, an unexpected lower B cell expansion measured by flow cytometry, despite a secondary antibody response. We then analyzed CD4(+)CD25(+)Foxp3(+) regulatory T cells (Tregs) and CD4(+)CD25(+)Foxp3(-) helper T cells after in vitro (re)stimulation of mesenteric lymph node cells …

T-LymphocytesHealth Toxicology and Mutagenesismedicine.medical_treatmentT cellBacterial ToxinsDose-Response Relationship Immunologiclcsh:Medicinechemical and pharmacologic phenomenaBiologyToxicologyArticleregulatory T cellsEnterotoxinsMiceInterleukin 21Immune systemB-1a lymphocyteAdjuvants ImmunologicAntigenmedicineAnimalsIL-2 receptorCD25B cellB-LymphocytesMice Inbred BALB CB lymphocytemucosal immunizationEscherichia coli Proteinslcsh:RRotavirus VaccinesVirionFOXP3LT-R192Ghemic and immune systemsrotavirusmedicine.anatomical_structureFoxp3ImmunologyFemaleImmunizationAdjuvantToxins
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Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor

2012

Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characteriza…

TASTE RECEPTORSucroseCircular dichroismcongenital hereditary and neonatal diseases and abnormalitiesProtein Conformation[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionumami receptorUmamiSWEETENERmedicine.disease_causeReceptors G-Protein-Coupledtaste03 medical and health sciencesGPCRTaste receptorPROTEIN REFOLDINGexpressionEscherichia colimedicineHumansRECOMBINANT GPCRbacteriaReceptorEscherichia coli030304 developmental biologyG protein-coupled receptorInclusion Bodies0303 health sciencesChemistrysweet receptor030302 biochemistry & molecular biologyRecombinant ProteinsTransmembrane proteinnervous system diseasesResearch NoteBACTERIAL EXPRESSIONBiochemistrysugarElectrophoresis Polyacrylamide GelHeterologous expression[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionrecombinant proteinProtein BindingBiotechnology
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Antimicrobial Effects Of The Ethanolic Extracts And Essential Oils Of Tanacetum Vulgare L From Romania

2015

Abstract This paper investigates the antimicrobial action of the extracts and essential oil of wildgrowing Tanacetum vulgare L on: Staphylococcus aureus, Escherichia coli, Pseudomonas aeruginosa and Bacilus subtilis, using the diffusion disc method. The essential oils but also the ethanolic extracts tested exhibited moderate action on Staphilococcus aureus and Bacillus subtilis and low action on E. coli and Pseudomonas aeruginosa. The moderate antimicrobial activity is related to the amount of some chemical components of the essential oil of T. vulgare flos. Thus, this paper presents also the quantitative and qualitative analysis of the essential oils of T. vulgare harvested from two differ…

Tanacetum vulgare L.biologyChemistryPseudomonas aeruginosaBacillus subtilisTP368-456Antimicrobialmedicine.disease_causebiology.organism_classificationIndustrial and Manufacturing Engineeringessential oilFood processing and manufacturelaw.inventionQualitative analysisStaphylococcus aureuslawantimicrobial effectsmedicinetanacetum vulgareFood scienceextractEscherichia coliEssential oilFood ScienceActa Universitatis Cibiniensis. Series E: Food Technology
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Evaluation of dermal toxicity of antibacterial cotton textile coated by sol-gel technology

2017

AbstractThis paper reports about cotton textile modification by sol-gel technology with the purpose of obtaining antibacterial properties, evaluation of antibacterial properties and dermal toxicity tests of cotton textile with Zn and Si coating. Antibacterial properties evaluation against pathogenic microorganisms Pseudomonas aeruginosa, Staphylococcus aureus, and Escherichia coli made using the Parallel streak method in accordance with ATCC147 standard. For more specific evaluation of the coated textile, in vitro cytotoxicity test with epidermal HaCat cells was done. It is concluded that the coatings containing Zn and Si obtained by the sol-gel technology can impart antibacterial propertie…

TextilePolymers and PlasticsMaterials Science (miscellaneous)Microorganism02 engineering and technologyengineering.materialmedicine.disease_cause01 natural sciencesIndustrial and Manufacturing EngineeringCoating0103 physical sciencesmedicineFood scienceComposite materialEscherichia coli010302 applied physicsintegumentary systembiologyChemistrybusiness.industryPathogenic bacteria021001 nanoscience & nanotechnologybiology.organism_classificationHaCaTStaphylococcus aureusengineering0210 nano-technologyGeneral Agricultural and Biological SciencesbusinessBacteriaThe Journal of The Textile Institute
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Combining in the melt physical and biological properties of poly(caprolactone) and chlorhexidine to obtain antimicrobial surgical monofilaments.

2012

Bacterial infections on a sutured wound represent a critical problem, and the preparation of suture threads possessing antimicrobial properties is valuable. In this work, poly(caprolactone) (PCL) monofilaments were compounded at the concentration of 1, 2 and 4 % (w/w), respectively, to the antiseptic chlorhexidine diacetate (CHX). The incorporation was carried out in the melt by a single-step methodology, i.e. “online” approach. Mechanical tests revealed that the incorporation of CHX does not significantly change tensile properties of PCL fibres as the thermal profile adopted to prepare the compounded fibres does not compromise the antibacterial activity of CHX. In fact, CHX confers to comp…

Thermoplasticmedicine.drug_classCell SurvivalPolyestersSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and Biotechnologychemistry.chemical_compoundAntisepticTensile StrengthPolymer chemistryUltimate tensile strengthmedicineEscherichia coliHumanschemistry.chemical_classificationpoly(caprolactone)biologyChemistryChlorhexidinechlorhexidineChlorhexidineSuture TechniquesSpectrometry X-Ray EmissionGeneral MedicineFibroblastsbiology.organism_classificationAntimicrobialMicrococcus luteusSettore ING-IND/22 - Scienza E Tecnologia Dei MaterialiEquipment and Suppliessurgical monofilamentsAnti-Infective Agents LocalMicroscopy Electron ScanningMicrococcus luteusAntibacterial activityCaprolactoneBiotechnologyNuclear chemistrymedicine.drugBacillus subtilisApplied microbiology and biotechnology
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Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force

2012

ABSTRACT Thiosulfate respiration in Salmonella enterica serovar Typhimurium is catalyzed by the membrane-bound enzyme thiosulfate reductase. Experiments with quinone biosynthesis mutants show that menaquinol is the sole electron donor to thiosulfate reductase. However, the reduction of thiosulfate by menaquinol is highly endergonic under standard conditions (Δ E °′ = −328 mV). Thiosulfate reductase activity was found to depend on the proton motive force (PMF) across the cytoplasmic membrane. A structural model for thiosulfate reductase suggests that the PMF drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase was able to catalyze the combined …

ThiosulfatesSulfurtransferaseElectron donorNaphtholsBiologyPhotochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundElectron transferSulfiteEscherichia coliFormateMolecular BiologyExergonic reactionThiosulfateTerpenesChemiosmosisProton-Motive ForceSalmonella entericaGene Expression Regulation BacterialArticleschemistryBiochemistrySulfurtransferasesThermodynamicsProtonsOxidation-ReductionJournal of Bacteriology
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Fluorescence Properties of the Chromophore-Binding Domain of Bacteriophytochrome from Deinococcus radiodurans

2013

Fluorescent proteins are versatile tools for molecular imaging. In this study, we report a detailed analysis of the absorption and fluorescence properties of the chromophore-binding domain from Deinococcus radiodurans and its D207H mutant. Using single photon counting and transient absorption techniques, the average excited state lifetime of both studied systems was about 370 ps. The D207H mutation slightly changed the excited state decay profile but did not have a considerable effect on the average decay time of the system or the shape of the absorption and emission spectra of the biliverdin chromophore. We confirmed that the fluorescence properties of both samples are very similar in vivo…

Time FactorsFluorescence in the life sciencesPhotochemistrychemistry.chemical_compoundBimolecular fluorescence complementationBacterial ProteinsEscherichia coliMaterials ChemistryPhysical and Theoretical Chemistryta116BiliverdinbiologyPhytochromeBiliverdineta1182Deinococcus radioduransChromophorebiology.organism_classificationFluorescenceRecombinant ProteinsProtein Structure TertiarySurfaces Coatings and FilmschemistryMutationQuantum TheorySpectrophotometry UltravioletDeinococcusBinding domainThe Journal of Physical Chemistry B
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Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro

2002

The two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C(4)-dicarboxylate metabolism in response to extracellular C(4)- dicarboxylates such as fumarate or succinate. DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane. The intact DcuS protein (His(6)-DcuS) was overproduced and isolated in detergent containing buffer. His(6)-DcuS was reconstituted into liposomes made from E. coli phospholipids. Reconstituted His(6)-DcuS catalyzed, in contrast to the detergent-solubilized sensor, autophosphorylation by [gamma-(33)P]ATP with an approximate K(D) of 0.16 mm for ATP. Up t…

Time FactorsHistidine KinaseProteolipidsDetergentsBiologymedicine.disease_causeModels BiologicalBiochemistryAdenosine TriphosphateFumaratesEscherichia colimedicinePhosphorylationPromoter Regions GeneticProtein kinase AMolecular BiologyEscherichia coliDose-Response Relationship DrugKinaseEscherichia coli ProteinsCell MembraneAutophosphorylationDNACell BiologyTransmembrane proteinDNA-Binding ProteinsKineticsResponse regulatorBiochemistryLiposomesPhosphorylationSignal transductionProtein KinasesProtein BindingSignal TransductionTranscription FactorsJournal of Biological Chemistry
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