Search results for "(Escherichia coli)"

showing 10 items of 689 documents

Development of a biosensor for copper detection in aqueous solutions using an Anemonia sulcata recombinant GFP.

2014

Fluorescent proteins from marine organisms represent potential candidates for biosensor development. In this paper, we described the isolation of a native green fluorescent protein from Anemonia sulcata and the cloning and purification of its equivalent as a recombinant protein in Escherichia coli. Furthermore, the spectroscopic behaviours of the native and recombinant GFPs were investigated as a function of Cu2+, Cd2+, Pb 2+ and Ni2+ concentration. Our results suggest the high selectivity of both proteins at copper than the other metals and, for the recombinant protein, a great sensitivity at a very low concentration (0.1-1 μM). Moreover, starting from these data, using the combination of …

Recombinant proteinGreen Fluorescent Proteinschemistry.chemical_elementBioengineeringBiosensing Techniquesmedicine.disease_causeApplied Microbiology and BiotechnologyBiochemistrylaw.inventionGreen fluorescent proteinlawQuenchingmedicineEscherichia coliAnimalsGreen fluorescent proteinMolecular BiologyEscherichia coliQuenching (fluorescence)Aqueous solutionChromatographyChemistryDivalent metal ionCopper; Detector; Divalent metal ions; Green fluorescent protein; Quenching; Recombinant proteinDetectorGeneral MedicineFluorescenceCopperSea AnemonesRecombinant DNABiosensorCopperBiotechnologyApplied biochemistry and biotechnology
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Production of biologically active light chain of tetanus toxin inEscherichia coli

1993

AbstractThe activity of the light (L) chain of tetanus toxin, and of mutants constructed by site-directed mutagenesis, was studied by expression and purification of the proteins from E. coli. Wild-type recombinant L chain (pTet87) was active in the inhibition of exocytosis from cultured bovine adrenal chromaffin cells, although at a level 5–15% of that of L chain purified from tetanus toxin. L chain mutants which terminated at Leu-438 (pTet89), or which contained a Cys-to-Ser mutation at residue 439 (pTet88) were equally as active as the full-length recombinant protein. The reduced activity of pTet87 L chain correlated with C-terminal proteolysis of the protein upon purification. A tryptic …

Recombinant proteinMacromolecular SubstancesProteolysisMolecular Sequence DataRestriction MappingDNA RecombinantBiophysicsBiologymedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosislaw.inventionNorepinephrineTetanus ToxinStructural BiologylawEscherichia coliGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularSite-directed mutagenesisMolecular BiologyEscherichia coliCells Culturedchemistry.chemical_classificationBase Sequencemedicine.diagnostic_testToxinBiological activityCell BiologyMolecular biologyRecombinant ProteinsE. coli Chromaffin cellAmino acidKineticsOligodeoxyribonucleotideschemistryBiochemistryAdrenal MedullaMutagenesis Site-DirectedRecombinant DNACalciumCattleElectrophoresis Polyacrylamide GelSite directed mutagenesisFEBS Letters
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Oxygen regulated gene expression in facultatively anaerobic bacteria

1994

In facultatively anaerobic bacteria such as Escherichia coli, oxygen and other electron acceptors fundamentally influence catabolic and anabolic pathways. E. coli is able to grow aerobically by respiration and in the absence of O2 by anaerobic respiration with nitrate, nitrite, fumarate, dimethylsulfoxide and trimethylamine N-oxide as acceptors or by fermentation. The expression of the various catabolic pathways occurs according to a hierarchy with 3 or 4 levels. Aerobic respiration at the highest level is followed by nitrate respiration (level 2), anaerobic respiration with the other acceptors (level 3) and fermentation. In other bacteria, different regulatory cascades with other underlyin…

Regulation of gene expressionAnaerobic respirationAnabolismCellular respirationGene Expression Regulation BacterialGeneral MedicineBiologymedicine.disease_causeMicrobiologyAerobiosisElectron TransportOxygenBacteria AnaerobicOxidative StressGlucoseBiochemistrymedicineFermentationAnaerobiosisAnaerobic bacteriaEnergy MetabolismMolecular BiologyEscherichia coliAnaerobic exerciseNitritesAntonie van Leeuwenhoek
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Current research in biotechnology: Exploring the biotech forefront

2019

Abstract Biotechnology is an evolving research field that covers a broad range of topics. Here we aimed to evaluate the latest research literature, to identify prominent research themes, major contributors in terms of institutions, countries/regions, and journals. The Web of Science Core Collection online database was searched to retrieve biotechnology articles published since 2017. In total, 12,351 publications were identified and analyzed. Over 8500 institutions contributed to these biotechnology publications, with the top 5 most productive ones scattered over France, China, the United States of America, Spain, and Brazil. Over 140 countries/regions contributed to the biotechnology resear…

Research literaturebusiness.industrylcsh:BiotechnologyOnline databaseSaccharomyces cerevisiaeBiotechnologylcsh:TP248.13-248.65Political scienceEscherichia coliNanotechnologyNanoparticlesBiotechnology researchChinabusinessMetabolic engineeringBioremediationBiotechnology
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B subunits of cholera toxin and thermolabile enterotoxin of Escherichia coli have similar adjuvant effect as whole molecules on rotavirus 2/6-VLP spe…

2015

The purpose of this study was to evaluate the adjuvant effect of the B subunits of cholera toxin (CT) and the thermolabile enterotoxin of Escherichia coli (LT) by the intrarectal route of immunization and compare them to the whole molecules CT and LT-R192G, a non toxic mutant of LT, using 2/6-VLP as an antigen, in mice. All molecules induced similar antigen specific antibody titers in serum and feces, whereas different T cell profiles were observed. CTB and LTB, conversely to CT and LT-R192G, did not induce detectable production of IL-2 by antigen specific T cells. Moreover, CTB, conversely to LT-R192G, CT and LTB, did not induce antigen specific CD4+CD25+Foxp3- and Foxp3+ T cells, thus sho…

RotavirusCholera Toxin[SDV]Life Sciences [q-bio]T cellmedicine.medical_treatmentBacterial ToxinsEnterotoxinBiologymedicine.disease_causeAntibodies ViralMicrobiologyAntibodiesMicrobiologyB subunitEnterotoxinsFecesMiceAntigenAdjuvants ImmunologicImmunologicAdministration RectalmedicineAnimalsViralAdjuvantsIL-2 receptorVaccines Virus-Like ParticleThermolabileB cellVaccinesIntrarectalEscherichia coli ProteinsCholera toxinRotavirus VaccinesLT-R192G3. Good healthVirus-Like ParticleInfectious Diseasesmedicine.anatomical_structureAdministrationAntibody FormationInterleukin-2Th17 CellsImmunizationRectalAdjuvantImmunologic MemoryMicrobial pathogenesis
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Different profile and distribution of antigen specific T cells induced by intranasal and intrarectal immunization with rotavirus 2/6-VLP with and wit…

2013

International audience; In this study, we compared both the profile and distribution of antigen specific primed T cells after intrarectal (IR) and intranasal (IN) immunization with rotavirus (RV) 2/6-VLP, alone or in the presence of LT-R192G, in order to highlight the differences between the two routes and the impact of the adjuvant. Adult BALB/c mice were immunized once with 2/6-VLP with or without adjuvant and the T cell response was analyzed in lymphoid tissues after in vitro restimulation with the antigen. IN, but not IR, immunization of mice with 2/6-VLP alone induced antigen-specific IL-10 and IL-17 secreting T cells. IL-10-, in contrast to IL-17-, secreting T cells did not migrate to…

Rotavirusmedicine.medical_treatmentT-Lymphocytes[SDV]Life Sciences [q-bio]Priming (immunology)DistributionPHENOTYPEPROTECTSEnterotoxins0302 clinical medicineCell MovementINFECTIONMesenteric lymph nodesHEAT-LABILE TOXINIMMUNE-RESPONSEIL-2 receptorAntigens Viral0303 health sciencesB-LymphocytesMice Inbred BALB CIntrarectalEscherichia coli ProteinsVaccinationFOXP3CHOLERA-TOXINLT-R192G3. Good healthInfectious Diseasesmedicine.anatomical_structureIntranasal030220 oncology & carcinogenesisMolecular MedicineFemaleAdjuvantLymphoid TissueT cellBacterial ToxinsSpleenBiologyMUCOSAL VACCINESRotavirus Infections03 medical and health sciencesCross-PrimingAntigenAdjuvants ImmunologicAdministration RectalVIRUS-LIKE PARTICLESmedicineAnimalsVaccines Virus-Like ParticleImmunity MucosalAdministration Intranasal030304 developmental biologyGeneral VeterinaryGeneral Immunology and MicrobiologyInterleukinsPublic Health Environmental and Occupational HealthRotavirus VaccinesT cellMICEImmunologyCHALLENGE
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Role of glycine-82 as a pivot point during the transition from the inactive to the active form of the yeast Ras2 protein

1991

AbstractRas proteins bind either GDP or GTP with high affinity. However, only the GTP-bound form of the yeast Ras2 protein is able to stimulate adenylyl cyclase. To identify amino acid residues that play a role in the conversion from the GDP-bound to the GTP-bound state of Ras proteins, we have searched for single amino acid substitutions that selectively affected the binding of one of the two nucleotides. We have found that the replacement of glycine-82 of the Ras2 protein by serine resulted in an increased rate of dissociation of Gpp(NH)p, a nonhydrolysable analog of GTP, while the GDP dissociation rate was not significantly modified. Glycine-82 resides in a region that is highly conserve…

Saccharomyces cerevisiae ProteinsGTP'Guanosine diphosphateProtein ConformationRestriction MappingGlycineBiophysicsSaccharomyces cerevisiaeBiochemistryFungal ProteinsGTP-binding protein regulatorsProtein structureGTP-Binding ProteinsStructural BiologyEscherichia coliGeneticsRHO protein GDP dissociation inhibitorAmino Acid SequenceRas2Binding siteMolecular BiologyPeptide sequencechemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesPoint mutationChemistryCell BiologyGuanosine triphosphateRecombinant ProteinsAmino acidModels StructuralBiochemistryMutagenesis Site-Directedras ProteinsS. cerevisaePlasmidsRasFEBS Letters
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Energetic aspects of intramolecular coupling between the nucleotide binding site and the distal switch II region of the yeast RAS2 protein

1994

AbstractWe have studied the interaction of the yeast RAS2 protein with guanine nucleotides using energetic parameters for the dissociation of RAS·nucleotide complexes. The results indicated that a Gly → Ser substitution at position 82 led to an altered interaction with GppNHp and, to a lesser extent, also with GDP. It was also possible to conclude that structural perturbation of Gly82 can stimulate nucleotide release by decreasing the energetic barrier for nucleotide dissociation. This, together with the observation that residues 80 and 81 are involved in the response of RAS to nucleotide exchange factors without affecting GDP binding per se, suggests a potential mechanism for exchange fact…

Saccharomyces cerevisiae ProteinsStereochemistryCdc25GuanineSaccharomyces cerevisiaeGlycineBiophysicsSaccharomyces cerevisiaeGuanosine DiphosphateBiochemistryFungal ProteinsStructure-Activity RelationshipSCD25chemistry.chemical_compoundGTP-Binding ProteinsStructural BiologyEscherichia coliSerineGeneticsNucleotideBinding siteRas2Molecular Biologychemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesCDC25biologyGDP bindingTemperatureCell Biologybiology.organism_classificationGuanine NucleotidesRecombinant ProteinsYeastchemistryras ProteinsGDP exchange factorbiology.proteinThermodynamicsRASFEBS Letters
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A natural A/T-rich sequence from the yeast FBP1 gene exists as a cruciform in Escherichia coli cells.

1993

Abstract Palindromic or semipalindromic sequences can adopt cruciform structures in DNA in vitro. It has been demonstrated in some cases that A/T-rich cruciforms exist also in vivo in Escherichia coli. The biological function of those structures is not understood although putative cruciforms have been found in interesting locations on replication origins, operators, or transcriptional termination regions. Here we show by means of the use of structure-dependent nucleases that the 3′ end of the yeast FBP1 gene contains a stable cruciform both in vitro and in E. coli cells and that in both cases, its extrusion depends on the DNA supercoiling state.

Saccharomyces cerevisiaeGenes FungalMolecular Sequence DataDNA RecombinantSaccharomyces cerevisiaeOrigin of replicationmedicine.disease_causechemistry.chemical_compoundmedicineEscherichia coliMolecular BiologyGeneEscherichia coliPalindromic sequenceGeneticsEndodeoxyribonucleasesbiologyBase SequenceDNA Superhelicalbiology.organism_classificationCell biologychemistryCruciformDNA supercoilNucleic Acid ConformationDNAPlasmid
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S. Typhimurium virulence changes caused by exposure to different non-thermal preservation treatments using C. elegans

2017

The aims of this research study were: (i) to postulate Caenorhabditis elegans (C. elegans) as a useful organism to describe infection by Salmonella enterica serovar Typhimurium (S. Typhimurium), and (ii) to evaluate changes in virulence of S. Typhimurium when subjected repetitively to different antimicrobial treatments. Specifically, cauliflower by-product infusion, High Hydrostatic Pressure (HHP), and Pulsed Electric Fields (PEF). This study was carried out by feeding C. elegans with different microbial populations: E. coli OP50 (optimal conditions), untreated S. Typhimurium, S. Typhimurium treated once and three times with cauliflower by-product infusion, S. Typhimurium treated once and f…

Salmonella typhimurium0301 basic medicineSerotype030106 microbiologyHydrostatic pressureVirulenceBrassicaMicrobiologyMicrobiologyFoodborne Diseases03 medical and health sciences0404 agricultural biotechnologyPulsed Electric FieldsEscherichia coliHydrostatic PressureAnimalsCaenorhabditis elegansCaenorhabditis elegansVirulencebiologyBayes Theorem04 agricultural and veterinary sciencesGeneral Medicinebiology.organism_classificationAntimicrobial040401 food scienceAnti-Bacterial AgentsDisease Models AnimalBayesian survival analysisHigh Hydrostatic PressureSalmonella entericaSalmonella InfectionsbacteriaAntimicrobialPlant PreparationsS typhimuriumFood ScienceInternational Journal of Food Microbiology
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