Search results for "Escher"

showing 10 items of 728 documents

Integron and genotype patterns of quinolones-resistant uropathogenic Escherichia coli

2011

Uropathogenic Escherichia coli are the most common cause of urinary tract infections,and quinolones-resistant strains cause growing concern in developing countries. This study provides relevant data in relation to the molecular epidemiology of these isolateswith respect to the distribution of integron among them and in doing so, to control the infections and adopt efficient strategies. This study was performed on 96 strains of E. coliisolated from patients with community acquired urinary tract infections in Jahrom, Iran. Having determined the antibiotic susceptibility patterns, isolates were resistant to quinolones (Ciprofloxacin, Norfloxacin and Nalidixic acid) screened for integron classe…

Settore MED/07 - Microbiologia E Microbiologia ClinicaMolecular epidemiologyNalidixic acidQuinolones-resistant uropathogenic escherichia coliPlant Sciencebiochemical phenomena metabolism and nutritionBiologybacterial infections and mycosesmedicine.disease_causeIntegronMicrobiologyVirologyIntegronMicrobiologyCiprofloxacinInfectious DiseasesGenotypemedicinebiology.proteinPulsed-field gel electrophoresisbacteriaEscherichia coliPulsed field gel electrophoresiNorfloxacinmedicine.drug
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Two Patients With History of STEC-HUS, Posttransplant Recurrence and Complement Gene Mutations

2013

Hemolytic uremic syndrome (HUS) is a disease of microangiopathic hemolytic anemia, thrombocytopenia and acute renal failure. About 90% of cases are secondary to infections by Escherichia coli strains producing Shiga-like toxins (STEC-HUS), while 10% are associated with mutations in genes encoding proteins of complement system (aHUS). We describe two patients with a clinical history of STEC-HUS, who developed end-stage renal disease (ESRD) soon after disease onset. They received a kidney transplant but lost the graft for HUS recurrence, a complication more commonly observed in aHUS. Before planning a second renal transplantation, the two patients underwent genetic screening for aHUS-associat…

Shiga-toxinGraft RejectionMaleDNA Primer030232 urology & nephrologyEscherichia coli InfectionGene mutationurologic and male genital diseasesGastroenterology0302 clinical medicineRecurrenceRisk Factorshemic and lymphatic diseasesImmunology and AllergyPharmacology (medical)gene mutationKidney transplantationEscherichia coli Infections0303 health sciencesKidneymedicine.diagnostic_testShiga-Toxigenic Escherichia coliAntigens CD46Microangiopathic hemolytic anemiaMiddle AgedPrognosisfemale genital diseases and pregnancy complications3. Good healthPedigreemedicine.anatomical_structureComplement Factor IComplement factor I; gene mutation; hemolytic uremic syndrome; kidney transplantation; membrane cofactor protein; Shiga-toxin; Adult; Antigens CD46; Case-Control Studies; Complement Factor I; DNA Primers; Escherichia coli Infections; Female; Genetic Testing; Graft Rejection; Hemolytic-Uremic Syndrome; Heterozygote; Humans; Kidney Failure Chronic; Kidney Transplantation; Male; Middle Aged; Mutation; Pedigree; Prognosis; Recurrence; Risk Factors; Shiga-Toxigenic Escherichia coli; Thrombocytopenia; Young Adult; Transplantation; Immunology and Allergy; Pharmacology (medical)FemaleCase-Control StudieHumanAdultmedicine.medical_specialtyHeterozygotePrognosiComplement factor IMembrane Cofactor Protein03 medical and health sciencesYoung AdultInternal medicinemedicineHumansGenetic Testing030304 developmental biologyGenetic testingDNA PrimersTransplantationbusiness.industryCD46Risk Factormedicine.diseaseKidney TransplantationThrombocytopeniaTransplantationCase-Control StudiesImmunologyHemolytic-Uremic SyndromeMutationhemolytic uremic syndromeKidney Failure ChronicbusinessAmerican Journal of Transplantation
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Iron-binding compounds and related outer membrane proteins in Vibrio cholerae non-O1 strains from aquatic environments

1990

A total of 156 strains of Vibrio cholerae non-O1 from aquatic origins were examined for the presence of iron uptake mechanisms and compared with O1 strains and other Vibrio species. All non-O1 strains were able to grow in iron-limiting conditions, with MICs of ethylenediaminedi (O-hydroxyphenylacetic acid) ranging from 20 microM to 2 mM. The production of siderophores was demonstrated by growth in chrome azurol S agar and cross-feeding assays. All strains produced phenolate-type compounds, as assessed by the chemical tests and by bioassays with Salmonella typhimurium enb-7. Some of the strains also promoted the growth of S. typhimurium enb-1 (which can use only enterobactin as a siderophore…

SiderophoreVibrio anguillarumChromatography PaperIronBiological Transport ActiveSiderophoresBiologymedicine.disease_causeIron Chelating AgentsApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundEnterobactinVibrio cholerae non-O1VibrionaceaemedicineSerotypingEscherichia coliVibrio choleraeEcologybiology.organism_classificationchemistryBiochemistryVibrio choleraeSpectrophotometryVibriobactinWater MicrobiologyFood ScienceBiotechnologyBacterial Outer Membrane ProteinsResearch Article
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Complete sequence, expression and evolution of two members of the hexamerin protein family during the larval development of the rice moth, Corcyra ce…

2002

Three distinct types of storage hexamerins are expressed in the "last-instar" larvae of the rice moth, Corcyra cephalonica. A cDNA expression library was constructed from fat body-RNA and screened with a polyclonal antibody raised against purified hexamerin (SP2) of Corcyra cephalonica. Two slightly different "full-length" hexamerin cDNA clones (Hex2a and Hex2b) were isolated and sequenced. Both include open reading frames of 2109 bp which are translated into polypeptides of 703 amino acids with 92.5% identity. Signal peptides of 19 amino acids are present at the N-termini. The 684 amino acids native proteins have a high content of aryl groups (17.6%). According to both the criteria for ami…

Signal peptideDNA ComplementaryProtein familyBlotting WesternMolecular Sequence DataMothsBiochemistryEvolution MolecularComplete sequenceComplementary DNAEscherichia coliAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino AcidbiologyfungiBlotting Northernbiology.organism_classificationRecombinant ProteinsAmino acidOpen reading framechemistryBiochemistryRice mothLarvaInsect ScienceInsect ProteinsInsect Biochemistry and Molecular Biology
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A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica.

1996

A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector lambda gt 11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is …

Signal peptideDNA ComplementaryTranscription GeneticHydrolasesBlotting WesternGenetic VectorsMolecular Sequence DataRestriction MappingBioengineeringApplied Microbiology and BiotechnologyBiochemistryCell wallFungal ProteinsOpen Reading FramesTransformation GeneticCell WallComplementary DNAGene Expression Regulation FungalYeastsGeneticsEscherichia coliAmino Acid SequenceCloning MolecularFluorescent Antibody Technique IndirectPeptide sequenceAntibodies FungalGene LibraryExpression vectorbiologyBase SequencecDNA libraryRNASodium Dodecyl SulfateYarrowiaRNA Fungalbiology.organism_classificationBlotting NorthernBlotting SouthernBiochemistrySaccharomycetalesElectrophoresis Polyacrylamide GelBiotechnologyYeast (Chichester, England)
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Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli

2004

Chicken avidin is a highly popular tool with countless applications in the life sciences. In the present study, an efficient method for producing avidin protein in the periplasmic space of Escherichia coli in the active form is described. Avidin was produced by replacing the native signal sequence of the protein with a bacterial OmpA secretion signal. The yield after a single 2-iminobiotin–agarose affinity purification step was approx. 10 mg/l of virtually pure avidin. Purified avidin had 3.7 free biotin-binding sites per tetramer and showed the same biotin-binding affinity and thermal stability as egg-white avidin. Avidin crystallized under various conditions, which will enable X-ray cryst…

Signal peptideSpectrometry Mass Electrospray IonizationGlycosylationMolecular Sequence DataProtein Sorting Signalsmedicine.disease_causeBiochemistryAvian Proteinschemistry.chemical_compoundBacterial Proteinsstomatognathic systemTetramerAffinity chromatographymedicineAnimalsAmino Acid SequenceMolecular BiologyEscherichia coliEscherichia coli K12biologyCell BiologyPeriplasmic spacerespiratory systemAvidinMolecular WeightchemistryBiochemistryBiotinylationbiology.proteinChickensResearch ArticleBacterial Outer Membrane ProteinsAvidinBiochemical Journal
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F17-like fimbriae from an invasive Escherichia coli strain producing cytotoxic necrotizing factor type 2 toxin

1994

The F17b fimbriae encoded by the transmissible virulence plasmid Vir, also coding for cytotoxic necrotizing factor type 2, were characterized. A 5.7-kb region of Vir mediates in vitro N-acetylglucosamine-sensitive adhesion to calf intestinal villi. Sequence analysis revealed that this region codes for a structural subunit and an adhesin closely related to the F17-A and F17-G proteins encoded by the F17 fimbrial gene cluster. The F17b-A gene presents an open reading frame of 540 bp encoding a polypeptide of 180 amino acids with a putative signal peptide of 21 residues. The mature protein shows an identity of 74% with the F17-A structural subunit. This 20-kDa protein is recognized by antiseru…

Signal peptideVirulence Factors[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataImmunologyFimbriaMutantBiologymedicine.disease_causeMicrobiologyMicrobiologyBacterial ProteinsGene clusterEscherichia colimedicineAmino Acid SequenceEscherichia coliPeptide sequenceAdhesins Escherichia coliAntigens BacterialBase SequenceCytotoxinsEscherichia coli ProteinsSEQUENCE NULECOTIDIQUEbiochemical phenomena metabolism and nutritionMolecular biology[SDV] Life Sciences [q-bio]Bacterial adhesinOpen reading frameInfectious DiseasesFimbriae BacterialCLONAGE DE GENEParasitologyResearch ArticleBacterial Outer Membrane ProteinsPlasmidsInfection and Immunity
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Switchable Bactericidal Effects from Novel Silica-Coated Silver Nanoparticles Mediated by Light Irradiation

2011

Here we report on the triggering of antibacterial activity by a new type of silver nanoparticle coated with porous silica, Ag@silica, irradiated at their surface plasmon resonant frequency. The nanoparticles are able to bind readily to the surface of bacterial cells, although this does not affect bacterial growth since the silica shell largely attenuates the intrinsic toxicity of silver. However, upon simultaneous exposure to light corresponding to the absorption band of the nanoparticles, bacterial death is enhanced selectively on the irradiated zone. Because of the low power density used for the treatments, we discard thermal effects as the cause of cell killing. Instead, we propose that …

SilverSurface PropertiesUltraviolet RaysMetal NanoparticlesNanoparticleMineralogyMicrobial Sensitivity TestsBacterial growthSilver nanoparticleStructure-Activity RelationshipEscherichia coliElectrochemistryGeneral Materials ScienceIrradiationSpectroscopyAntibacterial agentDose-Response Relationship DrugChemistrySurface plasmonSurfaces and InterfacesSilicon DioxideCondensed Matter PhysicsAnti-Bacterial AgentsCell killingAbsorption bandBiophysicsLangmuir
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Small RNA‐binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli

2019

Abstract The RNA‐binding protein RapZ cooperates with small RNAs (sRNAs) GlmY and GlmZ to regulate the glmS mRNA in Escherichia coli. Enzyme GlmS synthesizes glucosamine‐6‐phosphate (GlcN6P), initiating cell envelope biosynthesis. GlmZ activates glmS expression by base‐pairing. When GlcN6P is ample, GlmZ is bound by RapZ and degraded through ribonuclease recruitment. Upon GlcN6P depletion, the decoy sRNA GlmY accumulates through a previously unknown mechanism and sequesters RapZ, suppressing GlmZ decay. This circuit ensures GlcN6P homeostasis and thereby envelope integrity. In this work, we identify RapZ as GlcN6P receptor. GlcN6P‐free RapZ stimulates phosphorylation of the two‐component sy…

Small RNAsmall regulatory RNAcell envelope precursor glucosamine‐6‐phosphatemedicine.disease_causenegative feedback loopmetabolite sensing0302 clinical medicinetwo-component system QseE-QseFRNA-binding protein RapZRNA‐binding protein RapZGlucosamine0303 health sciencesbiologyEscherichia coli ProteinsGeneral NeuroscienceRNA-Binding ProteinsArticlesRNA BiologyMicrobiology Virology & Host Pathogen InteractionReceptors AdrenergicCell biologyDNA-Binding ProteinsRNA BacterialTransfer RNAPhosphorylationCell envelopeSignal TransductionGlucose-6-PhosphateGeneral Biochemistry Genetics and Molecular BiologyArticletwo‐component system QseE‐QseF03 medical and health sciencesBacterial Proteinscell envelope precursorEscherichia colimedicineRNA MessengerRibonucleaseMolecular BiologyEscherichia coli030304 developmental biologyMessenger RNAGeneral Immunology and MicrobiologyBinding proteinsmall RNAs GlmY and GlmZGene Expression Regulation BacterialMicroreviewRNA binding proteincell envelope precursor glucosamine-6-phosphatetwo-component systembiology.proteinRNA Small Untranslated030217 neurology & neurosurgeryThe EMBO Journal
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Characterization of heat-labile toxin-subunit B from Escherichia coli by liquid chromatography-electrospray ionization-mass spectrometry and matrix-a…

2012

The possibilities of characterizing the heat-labile enterotoxin (LT) of enterotoxigenic Escherichia coli (ETEC) by liquid chromatography electrospray mass spectrometry (LC/ESI-MS) and matrix-assisted laser desorption with time-of-flight mass spectrometry (MALDI-TOF-MS) were investigated. The B subunit from recombinant E. coli (expression in Pichia pastoris) can be detected by LC/ESI-MS expressed in P. pastoris and the charge envelope signals can be observed; LC/ESI-MS and MALDI-TOF-MS analysis allowed the acquisition of labile toxin subunit B (LTB) molecular weight and preliminary structural characterization of LTB toxin. MALDI-TOF analysis after reduction and alkylation of the protein evid…

Spectrometry Mass Electrospray IonizationElectrospray ionizationProtein subunitBacterial ToxinsMolecular Sequence DataToxicologyMass spectrometrymedicine.disease_causespettroemtria di massaPichiaPichia pastorisEnterotoxinsProtein sequencingEnterotoxigenic Escherichia colimedicineTrypsinAmino Acid SequenceDisulfidesPhosphorylationEscherichia colitossinaChromatographyMolecular massbiologyChemistryEscherichia coli ProteinsE. coliGeneral Medicinebiology.organism_classificationRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationFood ScienceChromatography LiquidFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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