Search results for "outer"

showing 10 items of 252 documents

High affinity iron-uptake systems in Vibrio damsela: role in the acquisition of iron from transferrin

1997

In this work, the high affinity iron-acquisition systems displayed by virulent and avirulent strains of Vibrio damsela have been investigated. This species is an autochthonous member of marine ecosystems that can behave as an opportunistic pathogen for fish and mammals. All strains tested (i) were able to grow under the restricted conditions imposed by the iron chelators transferrin (Tf) and EDDHA, (ii) secreted siderophores of hydroxamic type, other than aerobactin and desferal, that were able to stimulate the growth of the auxotroph mutant Arthrobacter flavescens JG9, and (iii) expressed common iron-regulated outer membrane proteins (IROMPs). No change in LPS patterns was observed in resp…

SiderophoreChromatography PaperIronImmunoblottingBiological Transport ActiveSiderophoresVirulenceIron Chelating AgentsApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundVibrionaceaeVibriochemistry.chemical_classificationVirulencebiologyTransferrinGeneral Medicinebiology.organism_classificationVibriochemistryTransferrinAerobactinElectrophoresis Polyacrylamide GelWater MicrobiologyBacterial outer membraneBacteriaBacterial Outer Membrane ProteinsBiotechnologyJournal of Applied Microbiology
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Siderophores and related outer membrane proteins produced by pseudomonads isolated from eels and freshwater.

1992

A total of 46 environmental pseudomonads, together with six type strains, were examined for their siderophore-producing activity. All strains were able to grow under iron-limiting conditions, gave orange halos in the CAS agar assay, and produced hydroxamates, and some of them also produced phenolate-type compounds. Bioassays showed that all strains, except Pseudomonas aeruginosa, promoted growth of mutant strain Arthrobacter flavescens JG-9, deficient in hydroxamate production, and some of them promoted growth of Salmonella typhimurium enb-1, which requires enterobactin for growth. The presence of iron-regulated outer membrane proteins was observed, the molecular size of the main induced pr…

SiderophoreIronSiderophoresFresh WaterMicrobiologyMicrobiologychemistry.chemical_compoundEnterobactinSpecies SpecificityArthrobacterPseudomonasGeneticsAnimalsMolecular BiologyEelsbiologyPseudomonasbiology.organism_classificationMolecular WeightchemistryMembrane proteinBiochemistryBacterial outer membraneWater MicrobiologyBacteriaPseudomonadaceaeBacterial Outer Membrane ProteinsFEMS microbiology letters
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Siderophore-mediated iron acquisition mechanisms in Vibrio vulnificus biotype 2

1996

Vibrio vulnificus biotype 2 is a primary pathogen for eels and, as has recently been suggested, an opportunistic pathogen for humans. In this study we have investigated the ability of V. vulnificus biotype 2 to obtain iron by siderophore-mediated mechanisms and evaluated the importance of free iron in vibriosis. The virulence degree for eels was dependent on iron availability from host fluids, as was revealed by a reduction in the 50% lethal dose for iron-overloaded eels. This biotype produced both phenolate- and hydroxamate-type siderophores of an unknown nature and two new outer membrane proteins of around 84 and 72 kDa in response to iron starvation. No alterations in lipopolysaccharide …

SiderophoreIronSiderophoresVirulenceVibrio vulnificusApplied Microbiology and BiotechnologyMicrobiologyVibrionaceaeReceptors TransferrinAnimalsHumansPathogenVibriochemistry.chemical_classificationEelsVirulenceEcologybiologybiology.organism_classificationVibriochemistryBiochemistryTransferrinWater MicrobiologyBacterial outer membraneResearch ArticleBacterial Outer Membrane ProteinsFood ScienceBiotechnologyApplied and Environmental Microbiology
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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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Siderophores and related outer membrane proteins in Vibrio spp. which are potential pathogens of fish and shellfish

1991

. A total of eight reference strains and 43 environmental isolates of Vibrio species that are potential fish pathogens, were assayed for the production and utilization of siderophores. Chemical and biological assays indicated that all species produced phenolate compounds and only some strains of V. cholerae non-O1, V. parahaemolyticus and V. fluvialis produced hydroxamates. Bioassays indicated that all species produced compounds that stimulated the growth of the homologous and the heterologous species in low-iron media. The catechol-type siderophores produced may be functionally related to enterobactin as demonstrated by bioassays with enterobactin-deficient mutants. However, the chromatogr…

SiderophorebiologyVeterinary (miscellaneous)HeterologousAquatic Sciencebiology.organism_classificationVibrioMicrobiologychemistry.chemical_compoundEnterobactinchemistryBioassayAerobactinBacterial outer membraneShellfishJournal of Fish Diseases
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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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Analyse cartographique de données pédologiques et hydrogéologiques appliquée à la gestion responsable de produits phytosanitaires

2014

BASF launched a Responsible Bentazone Management plan in 2011, in order to preserve water resources and sustain its bentazon based herbicide solutions. This molecule is commercialized by the company for several years and is found at concentrations above the standard for drinking water in about 1% of groundwater catchments in France. The action plan aims to reduce contamination situations with recommendations on the use of bentazone (dose, timing of application, restrictions on vulnerable soils on groundwater catchment areas) that complement the commercialization authorization. The study carried out during the internship focused on the diagnosis of a groundwater catchment area located in the…

Soil scienceCartographyWater tableNappe d’eau souterraineGroundwater catchment areaContaminationCartographiePédologie[SDU.STU.HY] Sciences of the Universe [physics]/Earth Sciences/HydrologyProduits phytosanitaires[SDE.ES] Environmental Sciences/Environmental and SocietyPesticidesAire d’alimentation de captage
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Production of Norspermidine Contributes to Aminoglycoside Resistance in pmrAB Mutants of Pseudomonas aeruginosa

2019

Emergence of resistance to polymyxins in Pseudomonas aeruginosa is mainly due to mutations in two-components systems, that promote addition of 4-amino-4-deoxy-L-arabinose to the lipopolysaccharide (LPS) through upregulation of operon arnBCADTEF-ugd (arn) expression. Here, we demonstrate that mutations occurring in different domains of histidine kinase PmrB or in response regulator PmrA result in coresistance to aminoglycosides and colistin. All seventeen clinical strains tested exhibiting such a cross-resistance phenotype were found to be pmrAB mutants. As shown by gene deletion experiments, the decreased susceptibility of the mutants to aminoglycosides was independent from operon arn but r…

Spectrometry Mass Electrospray IonizationOperonSpermidineMutantMicrobial Sensitivity TestsMicrobiology03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsMechanisms of Resistance[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]PolyaminesPharmacology (medical)GeneComputingMilieux_MISCELLANEOUS030304 developmental biologyPharmacology0303 health sciences030306 microbiologyColistinNorspermidineHistidine kinaseGene Expression Regulation Bacterial[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyAnti-Bacterial AgentsResponse regulatorInfectious DiseasesAminoglycosideschemistryPseudomonas aeruginosaEffluxBacterial outer membraneTranscription Factors
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Molecular Co-operation between Protein PAM and Streptokinase for Plasmin Acquisition by Streptococcus pyogenes

1998

Bacterial surface-associated plasmin formation is believed to contribute to invasion, although the underlying molecular mechanisms are poorly understood. To define the components necessary for plasmin generation on group A streptococci we used strain AP53 which exposes an M-like protein ("PAM") that contains a plasminogen-binding sequence with two 13-amino acid residues long tandem repeats (a1 and a2). Utilizing an Escherichia coli-streptococcal shuttle vector, we replaced a 29-residue long sequence segment of Arp4, an M-like protein that does not bind plasminogen, with a single (a1) or the combined a1a2 repeats of PAM. When expressed in E. coli, the purified chimeric Arp/PAM proteins both …

Streptococcus pyogenesPlasminRecombinant Fusion Proteinsmedicine.medical_treatmentStreptokinasemedicine.disease_causeBiochemistryMicrobiologyBacterial Proteinsstomatognathic systemShuttle vectorTandem repeatEscherichiaparasitic diseasesmedicineStreptokinaseFibrinolysinMolecular BiologyGeneAntigens BacterialProteasebiologyPlasminogenCell Biologybiology.organism_classificationBiochemistryStreptococcus pyogenesTransformation BacterialCarrier ProteinsBacterial Outer Membrane Proteinsmedicine.drugJournal of Biological Chemistry
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