Search results for "Bacterial Protein"

showing 10 items of 616 documents

Diversity and Evolution of the Phenazine Biosynthesis Pathway

2010

ABSTRACT Phenazines are versatile secondary metabolites of bacterial origin that function in biological control of plant pathogens and contribute to the ecological fitness and pathogenicity of the producing strains. In this study, we employed a collection of 94 strains having various geographic, environmental, and clinical origins to study the distribution and evolution of phenazine genes in members of the genera Pseudomonas , Burkholderia , Pectobacterium , Brevibacterium , and Streptomyces . Our results confirmed the diversity of phenazine producers and revealed that most of them appear to be soil-dwelling and/or plant-associated species. Genome analyses and comparisons of phylogenies inf…

Antifungal Agentsgenome sequenceaeruginosa pao1virulence factorsphenazine-1-carboxylic acidVIRULENCE FACTORS GENE-CLUSTERApplied Microbiology and Biotechnologychemistry.chemical_compoundGene clusterEnvironmental MicrobiologyPhylogenySoil Microbiologyfluorescent pseudomonas2. Zero hungerGenetics0303 health sciencesEcologybiologyEPS-2PseudomonasPlants[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMultigene FamilyHorizontal gene transferBiotechnologyDNA BacterialWashingtonPectobacteriumGene Transfer HorizontalGenotypeSequence analysisMolecular Sequence DataPhenazineerwinia-herbicola eh1087pseudomonas-chlororaphis pcl1391Evolution Molecular03 medical and health sciencesBacterial ProteinsPseudomonasBotanyEscherichia coli030304 developmental biologyBacteriaBase SequencePSEUDOMONAS-CHLORORAPHIS030306 microbiologybiological-controlGene Expression Regulation BacterialSequence Analysis DNA15. Life on landbiology.organism_classificationrpoBERWINIA-HERBICOLAPHENAZINEBiosynthetic Pathwaysgene-clusterLaboratorium voor PhytopathologieBurkholderiachemistryGenes BacterialLaboratory of PhytopathologyPhenazinesburkholderia-cepacia complexSequence AlignmentFood Science
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Seeking the Source of Catalytic Efficiency of Lindane Dehydrochlorinase, LinA.

2020

Herein we present the results of an in-depth simulation study of LinA and its two variants. In our analysis, we combined the exploration of protein conformational dynamics with and without bound substrates (hexachlorocyclohexane (HCH) isomers) performed using molecular dynamics simulation followed by the extraction of the most frequently visited conformations and their characteristics with a detailed description of the interactions taking place in the active site between the respective HCH molecule and the first shell residues by using symmetry-adapted perturbation theory (SAPT) calculations. A detailed investigation of the conformational space of LinA substates has been accompanied by desc…

biologyChemistryActive siteLyasesInteraction energyLigand (biochemistry)Molecular mechanicsArticleSurfaces Coatings and FilmsMolecular dynamicsBacterial ProteinsComputational chemistryCatalytic DomainMaterials Chemistrybiology.proteinMoleculePhysical and Theoretical ChemistryPerturbation theoryPotential of mean forceHexachlorocyclohexaneThe journal of physical chemistry. B
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A Comparative Study on Nickel Binding to Hpn-like Polypeptides from Two Helicobacter pylori Strains

2021

Combined potentiometric titration and isothermal titration calorimetry (ITC) methods were used to study the interactions of nickel(II) ions with the N-terminal fragments and histidine-rich fragments of Hpn-like protein from two Helicobacter pylori strains (11637 and 26695). The ITC measurements were performed at various temperatures and buffers in order to extract proton-independent reaction enthalpies of nickel binding to each of the studied protein fragments. We bring up the problem of ITC results of nickel binding to the Hpn-like protein being not always compatible with those from potentiometry and MS regarding the stoichiometry and affinity. The roles of the ATCUN motif and multiple His…

QH301-705.5Glutaminenickel bindingCalorimetry<i>H. pylori</i>glutamine-richArticleCatalysisInorganic ChemistryBacterial ProteinsProtein DomainsNickelHistidinenickel binding; <i>H. pylori</i>; Hpn-like; histidine-rich; glutamine-rich; ATCUN motifAmino Acid SequenceBiology (General)Physical and Theoretical ChemistryQD1-999Molecular BiologySpectroscopyHelicobacter pyloriHpn-likeOrganic ChemistryGeneral Medicinehistidine-richATCUN motifComputer Science ApplicationsChemistryPotentiometryPeptidesH. pyloriInternational Journal of Molecular Sciences
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A New Niche for Anoxygenic Phototrophs as Endoliths

2018

ABSTRACT Anoxygenic phototrophic bacteria (APBs) occur in a wide range of aquatic habitats, from hot springs to freshwater lakes and intertidal microbial mats. Here, we report the discovery of a novel niche for APBs: endoliths within marine littoral carbonates. In a study of 40 locations around Isla de Mona, Puerto Rico, and Menorca, Spain, 16S rRNA high-throughput sequencing of endolithic community DNA revealed the presence of abundant phylotypes potentially belonging to well-known APB clades. An ad hoc phylogenetic classification of these sequences enabled us to refine the assignments more stringently. Even then, all locations contained such putative APBs, often reaching a significant pro…

0301 basic medicineChloroflexi (phylum)030106 microbiologyCarbonatesFresh WaterCyanobacteriaApplied Microbiology and BiotechnologyMicrobial Ecology03 medical and health sciencescarbonateBacteria AnaerobicAlgaemicrobiomesBacterial ProteinsPhylogenetics[ SDV.MP ] Life Sciences [q-bio]/Microbiology and ParasitologyChlorophytaRNA Ribosomal 16SMicrobial matAnaerobiosisintertidalPhotosynthesisBacteriochlorophyllsPhylogenygeographygeography.geographical_feature_categoryEcologybiologyPhototrophEcologybioerosionCoral ReefsMicrobiotaBioerosionCoral reefChloroflexibiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsAnoxygenic photosynthesisPhototrophic ProcessesFood ScienceBiotechnology
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Human kininogens interact with M protein, a bacterial surface protein and virulence determinant.

1995

Streptococcus pyogenes, the most significant streptococcal species in clinical medicine, expresses surface proteins with affinity for several human plasma proteins. Here we report that kininogens, the precursors to the vasoactive kinins, bind to the surface of S. pyogenes. M protein, a surface molecule and a major virulence factor-in these bacteria, occurs in &amp;gt; 80 different serotypes. Among 49 strains of S. pyogenes, all of different M serotypes, 41 bound radiolabelled kininogens, whereas 6 M protein-negative mutant strains showed no affinity. M protein of most serotypes bind fibrinogen, and among the 55 strains tested, binding of kininogens was closely correlated to fibrinogen bindi…

Kininogen bindingMyeloma proteinStreptococcus pyogenesM1 proteinMolecular Sequence DataEnzyme-Linked Immunosorbent Assaymedicine.disease_causeBiochemistryPeptide MappingAntibodiesBacterial ProteinsmedicineHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenAntigens BacterialBinding SitesbiologyVirulenceKininogensFibrinogen bindingFibrinogenCell BiologyLow-molecular-weight kininogenMolecular biologyStreptococcus pyogenesbiology.proteinCarrier Proteinscirculatory and respiratory physiologyResearch ArticleBacterial Outer Membrane ProteinsProtein Binding
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Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O

2001

The pore-forming toxin streptolysin O (SLO) can be used to reversibly permeabilize adherent and nonadherent cells, allowing delivery of molecules with up to 100 kDa mass to the cytosol. Using FITC-labeled albumin, 10 5 –10 6 molecules were estimated to be entrapped per cell. Repair of toxin lesions depended on Ca 2+ -calmodulin and on intact microtubules, but was not sensitive to actin disruption or to inhibition of protein synthesis. Resealed cells were viable for days and retained the capacity to endocytose and to proliferate. The active domains of large clostridial toxins were introduced into three different cell lines. The domains were derived from Clostridium difficile B-toxin and Clo…

rho GTP-Binding ProteinsCell Membrane PermeabilityGlycosylationCell SurvivalBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologymedicine.disease_causeCell LineBacterial ProteinsAlbuminsChlorocebus aethiopsTumor Cells CulturedmedicineAnimalsHumansSecretionParticle SizeActinMultidisciplinaryDose-Response Relationship DrugSecretory VesiclesProteinsBiological TransportDextransBiological SciencesActin cytoskeletonMolecular biologyRatsCell biologyCytosolImmunoglobulin GCOS CellsStreptolysinsras ProteinsClostridium botulinumStreptolysinProceedings of the National Academy of Sciences
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Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: the unknown connection

1994

Microbiology (medical)Microbial toxinsSeptic shockBacterial ToxinsImmunologySepsis syndromeGeneral MedicineBiologymedicine.diseasemedicine.disease_causeShock SepticIon ChannelsSystemic Inflammatory Response SyndromeMicrobiologyPathogenesisBacterial ProteinsStaphylococcus aureusShock (circulatory)ImmunologymedicineAnimalsHumansImmunology and Allergymedicine.symptomMedical Microbiology and Immunology
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Cutting Edge: An IL-17F-CreEYFP Reporter Mouse Allows Fate Mapping of Th17 Cells

2009

Abstract The need for reporter lines able to faithfully track Th17 cells in vivo has become an issue of exceptional importance. To address this, we generated a mouse strain in which Cre recombinase is expressed from the IL-17F promoter. Crossing the IL-17F-Cre allele to a conditional enhanced yellow fluorescent protein (EYFP) reporter mouse yielded the IL-17F-CreEYFP strain, in which IL-17F expression is twinned with EYFP in live IL-17F-expressing cells. Although we demonstrate that IL-17F expression is restricted to CD4+ T cells during experimental autoimmune encephalomyelitis, IL-17F-CreEYFP CD8 T cells robustly expressed IL-17F in response to TGF-β, IL-6, and IL-23. Fate mapping of IL-17…

Yellow fluorescent proteinAdoptive cell transferEncephalomyelitis Autoimmune ExperimentalRNA UntranslatedTransgeneImmunologyCre recombinaseMice TransgenicCD8-Positive T-LymphocytesT-Lymphocytes RegulatoryImmunophenotypingMiceBacterial ProteinsGenes ReporterFate mappingAnimalsHumansImmunology and AllergyCytotoxic T cellCells CulturedIntegrasesbiologyInterleukin-17ProteinsCell DifferentiationAdoptive TransferMolecular biologyPhenotypeIn vitroMice Inbred C57BLLuminescent ProteinsGene Expression RegulationMice Inbred DBAbiology.proteinThe Journal of Immunology
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Photobacterium damselae subsp. damselae Major Virulence Factors Dly, Plasmid-Encoded HlyA, and Chromosome-Encoded HlyA Are Secreted via the Type II S…

2015

ABSTRACT Photobacterium damselae subsp. damselae is a marine bacterium that causes septicemia in marine animals and in humans. Previously, we had determined a major role of pPHDD1 plasmid-encoded Dly (damselysin) and HlyA (HlyA pl ) and the chromosome-encoded HlyA (HlyA ch ) hemolysins in virulence. However, the mechanisms by which these toxins are secreted remain unknown. In this study, we found that a mini-Tn 10 transposon mutant in a plasmidless strain showing an impaired hemolytic phenotype contained an insertion in epsL , a component of a type II secretion system (T2SS). Reconstruction of the mutant by allelic exchange confirmed the specific involvement of epsL in HlyA ch secretion. In…

ErythrocytesTranscription GeneticVirulence FactorsImmunologyMutantVirulenceTransposasesBiologyGene MutantHemolysin ProteinsMicrobiologyHemolysisMicrobiologyHemolysin ProteinsMiceBacterial ProteinsEndopeptidasesAnimalsSecretionBacterial Secretion SystemsMice Inbred BALB CType II secretion systemBase SequencePhotobacteriumHemolysinBacterial InfectionsSequence Analysis DNAInfectious DiseasesPhotobacterium damselaeMutationParasitologyPlasmids
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Functional significance of membrane associated proteolysis in the toxicity of Bacillus thuringiensis Cry3Aa toxin against Colorado potato beetle.

2012

Abstract Bacillus thuringiensis Cry toxins are widely used as biocontrol agents in bioinsecticides and transgenic plants. In the three domain-Cry toxins, domain II has been identified as an important determinant of their highly specific activity against insects. In this work, we assessed the role in membrane associated proteolysis and toxicity in Colorado potato beetle (CPB) of a previously reported ADAM recognition motif present in Cry3Aa toxin domain II. We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 344, 346, 347, 351 and 353 of the ADAM recognition motif in Cry3Aa toxin. Cry3Aa toxin mutants displayed decreased toxicity when comp…

ProteasesColoradoProteolysisMutantBacillus thuringiensisToxicologymedicine.disease_causeMicrobiologyHemolysin ProteinsRecognition sequenceBacterial ProteinsBacillus thuringiensismedicineAnimalsAmino Acid SequencePest Control BiologicalCells Culturedbiologymedicine.diagnostic_testBacillus thuringiensis ToxinsMicrovilliToxinfungiColorado potato beetleWild typeSequence Analysis DNAbiology.organism_classificationColeopteraEndotoxinsBiochemistryProteolysisMutagenesis Site-DirectedToxicon : official journal of the International Society on Toxinology
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