Search results for " Outer"

showing 10 items of 129 documents

Israeli spotted fever Rickettsia in Sicilian Rhipicephalus sanguineus ticks [6]

2003

Arachnid VectorMicrobiology (medical)Settore MED/07 - Microbiologia E Microbiologia ClinicaInfectious DiseasesItalyAnimalEpidemiologyMolecular Sequence DataRickettsia InfectionRickettsiaBacterial Outer Membrane ProteinTick
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Protein Networks and Complexes in Photoreceptor Cilia

2007

Vertebrate photoreceptor cells are ciliated sensory cells specialized for single photon detection. The photoreceptor outer segment corresponds to the ciliary shaft of a prototypic cilium. In the outer segment compartment, the ciliary membrane is highly modified into membranous disks which are enveloped by the plasma membrane in rod cells. At these outer segment disks, the visual transduction cascade--a prototypical G-protein coupled receptor transduction pathway is arranged. The light sensitive outer segments are linked by the socalled connecting cilium with the inner segment, the photoreceptor compartment which contains all organelles necessary for cell metabolism. The connecting cilium co…

Axonememedicine.anatomical_structureIntraflagellar transportCiliummedicineBasal bodysense organsBiologyCiliary shaftPhotoreceptor outer segmentCiliary membranePhotoreceptor cellCell biology
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Presence of a capsule in Vibrio vulnificus biotype 2 and its relationship to virulence for eels

1993

Strains of Vibrio vulnificus biotype 2, isolated from internal organs of diseased European eels as pure cultures of opaque cells, together with some reference strains from Japanese eels, were used in this study. Spontaneous translucent-phase variants were obtained from the corresponding parent strains and compared for a variety of phenotypic traits related to virulence for eels. The rate of colony dissociation from opaque to translucent cells was higher (around 10(-2)) than that observed for translucent to opaque cells (10(-3) to 10(-4)). Electron microscopy with ruthenium red revealed the presence of a capsule of variable thickness on opaque cells, whereas translucent-type colonies had no …

Bacterial capsuleIronImmunologyVirulenceVibrio vulnificusMicrobiologyHemolysisMicrobiologyFish DiseasesVibrionaceaeAnimalsBacterial CapsulesVibrioEelsbiologyLethal doseTransferrinbiology.organism_classificationVibrioMicroscopy ElectronInfectious DiseasesVibrio InfectionsParasitologyBacterial outer membraneBacteriaBacterial Outer Membrane ProteinsPlasmidsResearch Article
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Usefulness of omp1 restriction mapping for avian Chlamydia psittaci isolate differentiation

1995

Abstract Sixty-five avian Chlamydia psittaci isolates collected worldwide, including 27 previously characterized reference strains, were analysed by restriction mapping of the major outer membrane protein gene ( omp1 ) obtained after DMA amplification by PCR. They were compared to 2 ruminant isolates, a feline pneumonitis and a guinea pig inclusion conjunctivitis (GPIC) isolate. According to their omp1 restriction patterns, avian strains were heterogeneous in that they exhibited 6 and 4 distinct patterns using Alu I and Mbo II restriction enzymes, respectively, thus defining 7 groups. However, 84% of the studied strains belonged to groups 1 to 4, which share a specific fragment triplet of 4…

Base pairGuinea PigsRestriction MappingAMPLIFICATION CHAINE POLYMERASEIn Vitro TechniquesMicrobiologyBirdsRestriction mapAnimalsMolecular BiologyGene[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyElectrophoresis Agar GelChlamydia psittaciGeneticsbiologyDNA–DNA hybridizationGene AmplificationGeneral Medicinebiology.organism_classificationRestriction enzyme[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyChlamydophila psittaciGenes BacterialGenetic markerCatsCattleRestriction fragment length polymorphismBacterial Outer Membrane Proteins
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BBE31 from the Lyme disease agent Borrelia burgdorferi, known to play an important role in successful colonization of the mammalian host, shows the a…

2019

Abstract Lyme disease is a tick-borne infection caused by Borrelia burgdorferi sensu lato complex spirochetes. The spirochete is located in the gut of the tick; as the infected tick starts the blood meal, the spirochete must travel through the hemolymph to the salivary glands, where it can spread to and infect the new host organism. In this study, we determined the crystal structures of the key outer surface protein BBE31 from B. burgdorferi and its orthologous protein BSE31 (BSPA14S_RS05060 gene product) from B. spielmanii. BBE31 is known to be important for the transfer of B. burgdorferi from the gut to the hemolymph in the tick after a tick bite. While BBE31 exerts its function by intera…

BiophysicsSpirochaetales InfectionsPlasma protein bindingTickProtein glutathionylationBiochemistryMicrobiologyGene product03 medical and health sciencesLyme diseaseparasitic diseasesHemolymphmedicineAnimalsHumansBorrelia burgdorferiMolecular Biology030304 developmental biologyAntigens BacterialLyme Disease0303 health sciencesIxodesbiology030306 microbiologybacterial infections and mycosesbiology.organism_classificationmedicine.diseaseGlutathioneIxodes scapularisBorrelia burgdorferiSpirochaetalesBacterial Outer Membrane ProteinsBiochimica et Biophysica Acta (BBA) - General Subjects
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Involvement of the Pseudomonas aeruginosa MexAB–OprM efflux pump in the secretion of the metallophore pseudopaline

2020

ABSTRACTThe ability for all organisms to acquire metals from their environment is essential for life. To overcome the metal restriction imposed by the host’s nutritional immunity, bacterial pathogens exploits the use of small high metal affinity molecules called metallophores. Metallophores are first synthetized in the cytoplasm, then secreted into the medium where they sequester the metal. The metal-metallophore complex is then imported into the bacterium following binding to dedicated cell surface receptors. Recently, a new family of metallophores has been discovered in pathogenic bacteria called staphylopine in Staphylococcus aureus and pseudopaline in Pseudomonas aeruginosa. Here, we ar…

Bodily Secretions[SDV]Life Sciences [q-bio]Microbial Sensitivity TestsBiologymedicine.disease_causeMicrobiology03 medical and health sciencesBacterial ProteinsIn vivoDrug Resistance Multiple BacterialpseudopalinemedicineInner membraneSecretionMolecular Biology030304 developmental biology0303 health sciencesMexAB–OprMBacteriametallophoreChemistry030306 microbiologyPseudomonas aeruginosaMembrane Transport Proteinsbiology.organism_classificationIn vitroCell biology[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyCytoplasmPseudomonas aeruginosaefflux pumpEffluxCell envelopeBacterial outer membraneOligopeptidesBacteriaBacterial Outer Membrane Proteins
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Susceptibility of Pseudomonas aeruginosa isolates to ceftazidime is unrelated to the expression of the outer membrane protein OprC.

1997

Previously, it has been postulated that the porin OprC facilitates the diffusion of ceftazidime through the outer membrane of Pseudomonas aeruginosa. To further investigate this claim, the outer membrane protein (OMP) profiles of 22 ceftazidime-susceptible clinical isolates were analyzed. No correlation was found between MIC values and the level of expression of OprC. Further, OprC was either undetectable or expressed in reduced amounts in 12 isolates. In contrast, OprF and OprE were present in all isolates studied. This study suggests that OprC is dispensable for the permeation of ceftazidime through the outer membrane of P. aeruginosa.

CeftazidimePorinsmedicine.disease_causePorinaCeftazidimeMicrobiologyBacterial ProteinsDrug DiscoverymedicineHumansPharmacology (medical)Antibacterial agentPharmacologybiologyPseudomonas aeruginosaGeneral Medicinebiology.organism_classificationCephalosporinsImipenemInfectious DiseasesOncologyMembrane proteinSpainPorinPseudomonas aeruginosaThienamycinsBacterial outer membranePseudomonadaceaemedicine.drugBacterial Outer Membrane ProteinsChemotherapy
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The translocation of signaling molecules in dark adapting mammalian rod photoreceptor cells is dependent on the cytoskeleton.

2008

In vertebrate rod photoreceptor cells, arrestin and the visual G-protein transducin move between the inner segment and outer segment in response to changes in light. This stimulus dependent translocation of signalling molecules is assumed to participate in long term light adaptation of photoreceptors. So far the cellular basis for the transport mechanisms underlying these intracellular movements remains largely elusive. Here we investigated the dependency of these movements on actin filaments and the microtubule cytoskeleton of photoreceptor cells. Co-cultures of mouse retina and retinal pigment epithelium were incubated with drugs stabilizing and destabilizing the cytoskeleton. The actin a…

Cell signalingCytochalasin Dgenetic structuresLightPaclitaxelPhalloidineDark AdaptationBiologyHeterocyclic Compounds 4 or More RingsMicrotubulesRetinaMiceStructural BiologyMicrotubuleRetinal Rod Photoreceptor CellsCytoskeletal drugsThiabendazolemedicineArrestinAnimalsTransducinCytoskeletonMicroscopy ImmunoelectronActinCytoskeletonVision OcularMice KnockoutRetinal pigment epitheliumArrestinHomozygoteCell BiologyDarknessRod Cell Outer Segmenteye diseasesActinsCell biologyMice Inbred C57BLActin CytoskeletonProtein Transportmedicine.anatomical_structureMicroscopy Fluorescencesense organsTransducinCell Migration AssaysSignal TransductionCell motility and the cytoskeleton
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The long-term cytoskeletal rearrangement induced by rabbit enteropathogenic Escherichia coli is Esp dependent but intimin independent.

1999

Attaching and effacing rabbit enteropathogenic Escherichia coli (REPEC) of the O103 serogroup adhere diffusely on HeLa cells and trigger a slow progressive cytopathic effect (CPE) characterized by the recruitment of vinculin and the assembly of actin stress fibres. In contrast to REPEC O103, the reference human EPEC strain E2348/69 is unable to trigger the CPE. In this study, we have shown first that the fimbrial adhesin AF/R2, which mediates the diffuse adhesion of REPEC O103, was not sufficient to induce the CPE capability upon E2348/69. Non-polar mutants of REPEC O103 for espA, espB, espD and eae were then constructed. The four mutants were unable to induce attaching and effacing lesions…

DNA BacterialMutantMolecular Sequence DataMicrobiologyBacterial AdhesionMicrobiology03 medical and health sciencesBacterial ProteinsEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliCytoskeletonAdhesins BacterialMolecular Biology[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyActinCytoskeleton030304 developmental biologyIntiminCytopathic effect0303 health sciencesAdhesins Escherichia colibiologyBase Sequence030306 microbiologyEscherichia coli ProteinsGenetic Complementation TestREARRANGEMENTbiochemical phenomena metabolism and nutritionVinculinBacterial adhesin[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyGenes Bacterialbiology.proteinRabbitsCarrier ProteinsBacterial Outer Membrane ProteinsHeLa CellsMolecular microbiology
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Enzyme-linked immunosorbent assay for detection of Aeromonas hydrophila serogroup O:19

2006

An enzyme-linked immunosorbent assay has been developed for the detection of Aeromonas hydrophila serogroup O:19 isolated from epizootics in eels. The enzyme-linked immunosorbent assay specificity was confirmed after testing A. hydrophila O:19 and non-O:19 strains from different origins, as well as other Aeromonas species and other fish pathogens such as Vibrio vulnificus biotype 2, V. furnisii, V. damsela, Yersinia ruckerii and Edwardsiella tarda. The detection limits for A. hydrophila O:19 cells were around 10(4)-10(5) cells/well. Artificially infected eels were analyzed and the immunodetection was confirmed by cultural methods. With this methodology A. hydrophila O:19 was successfully de…

Enzyme-Linked Immunosorbent AssayVibrio vulnificusYersiniaMicrobiologyMicrobiologyFish DiseasesBacterial ProteinsAntigenAgglutination TestsGeneticsAnimalsMolecular Biologychemistry.chemical_classificationEelsbiologyEdwardsiella tardabacterial infections and mycosesbiology.organism_classificationMolecular biologyAeromonas hydrophilaAeromonas speciesAeromonas hydrophilaEnzymechemistrybacteriaBacterial outer membraneFEMS Microbiology Letters
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