Search results for " Outer"

showing 10 items of 129 documents

BB0172, a Borrelia burgdorferi Outer Membrane Protein That Binds Integrin Α3Β1

2013

ABSTRACT Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using in vitro transcription/translation systems in the presence of microsomal …

Models MolecularProtein familyMolecular Sequence DataIntegrinBiologyModels BiologicalMicrobiologyBiotecnologiaMicrobiologyAmino Acid SequenceBorrelia burgdorferiAdhesins BacterialMolecular BiologyIntegrin alpha3beta1Borrelia Burgdorferi InfectionProteïnes de membranaIntegrin alpha3beta1Articlesbiology.organism_classificationCell biologyBacterial adhesinBorrelia burgdorferibiology.proteinMSCRAMMBacterial outer membraneSequence AlignmentBacterial Outer Membrane ProteinsProtein Binding
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Evidence for Myosin VIIa-Driven Transport of Rhodopsin in the Plasma Membrane of the Photoreceptor-Connecting Cilium

2007

Defects in the gene encoding for the unconventional myosin VIIa leads to human Usher syndrome 1B, the most common form of hereditary combined blindness and deafness. To determine cellular function of myosin VIIa, we have investigated the subcellular localization of myosin VIIa in spacial relation relationship to potentially interacting proteins in mammalian photoreceptor cells. Western blot analysis of the axonemal fraction of photoreceptor cells by Western blot show that myosin VIIa and actin, as well as opsin, were present in the ciliary portion of the photoreceptors. Improved immunoelectron microscopy revealed that in mammalian photoreceptor cells, myosin VIIa was localized at the membra…

Myosin light-chain kinasegenetic structuresbiologyPhotoreceptor Connecting CiliumImmunoelectron microscopymacromolecular substancesPhotoreceptor outer segmenteye diseasesCell biologyRhodopsinMyosinotorhinolaryngologic diseasesbiology.proteinsense organsCiliary membraneActin
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Rapid and specific detection of F17-related pilin and adhesin genes in diarrheic and septicemic Escherichia coli strains by multiplex PCR

1996

The F17-related adhesins are prevalent in Escherichia coli strains isolated from calves with diarrhea or septicemia and from lambs with nephropathy. The F17 family includes the F17a, F17b, F17c, and F111 fimbriae produced by bovine E. coli strains and the G agglutinin produced by human uropathogenic E. coli strains. An easy and inexpensive multiplex PCR method was developed to detect all the F17-related fimbriae and to identify four subtypes of structural subunit genes and two distinct subfamilies of adhesin genes by only two runs of amplification. A strict correlation was observed between the phenotypic assays and the multiplex PCR method when 166 pathogenic E. coli strains isolated from i…

OperonFimbriaBacteremiamedicine.disease_causePolymerase Chain ReactionPilusFimbriae ProteinsEscherichia coli InfectionsComputingMilieux_MISCELLANEOUS2. Zero hunger0303 health sciencesbiologyEnterobacteriaceae3. Good healthPhenotype[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMultigene FamilyFimbriae ProteinsBacterial Outer Membrane ProteinsResearch ArticleDiarrheaMicrobiology (medical)Gene Transfer HorizontalCattle DiseasesSheep DiseasesMicrobiology03 medical and health sciencesSpecies SpecificityOperonEscherichia colimedicineAnimalsHumansAdhesins BacterialEscherichia coli[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyDNA Primers030304 developmental biologyBacteriological TechniquesSheepBase Sequence030306 microbiologyTOXINE CNF2biochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFIMBRIAE F17Bacterial adhesinGenes BacterialPilinbiology.proteinbacteriaCattle
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Immunoelectron-microscopic localization of synaptophysin in the organ of Corti of the guinea pig.

1997

Synaptophysin has been localized previously in the mammalian cochlea at the light-microscopic level and in few reports by electron microscopy using either a preincubation procedure or the avidin-biotin reaction. Here we present results of the electron-microscopic analysis for postembedding immunoreactivity of synaptophysin in the cochlea of the guinea pig of LR-White-embedded samples. Strong synaptophysin immunoreactivity is located in the cytoplasm of the efferent nerve endings at the base of inner and outer hair cells. Besides this, some antibodies to synaptophysin were also identified in the cytoplasm of outer hair cells. To get more information about the cellular content of synaptophysi…

Pathologymedicine.medical_specialtyCytoplasmImmunoelectron microscopyImmunocytochemistryGuinea PigsSynaptophysinlaw.inventionGuinea piglawotorhinolaryngologic diseasesmedicineAnimalsInner earMicroscopy ImmunoelectronCochleaHair Cells Auditory InnerbiologyChemistryImmunohistochemistryHair Cells Auditory Outermedicine.anatomical_structurenervous systemOtorhinolaryngologyOrgan of CortiSynaptophysinbiology.proteinsense organsElectron microscopeORL; journal for oto-rhino-laryngology and its related specialties
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Meropenem Permeation through the Outer Membrane of <i>Pseudomonas aeruginosa</i> Can Involve Pathways Other than the OprD Porin Channel

1996

The outer membrane protein (OMP) OprD is the major channel through which carbapenems permeate the outer membrane of Pseudomonas aeruginosa. In this study, we analyzed the OMP profiles of several P. aeruginosa clinical isolates showing diminished susceptibility to imipenem while remaining susceptible to meropenem. All these isolates lacked OprD or showed a reduced expression of this porin. Susceptibility to meropenem was thus independent of the level of OprD expression, indicating that the antimicrobial could be taken up via an alternative route. The level of expression of OprC (70 kD) was also unrelated to meropenem susceptibility. Nevertheless, OMPs OprF and OprE were expressed by all isol…

PharmacologyImipenembiologyPseudomonas aeruginosaGeneral Medicinebiochemical phenomena metabolism and nutritionbacterial infections and mycosesbiology.organism_classificationmedicine.disease_causeMeropenemPorinaMicrobiologyInfectious DiseasesOncologyDrug DiscoveryPorinpolycyclic compoundsmedicinebacteriaPharmacology (medical)Bacterial outer membranemedicine.drugPseudomonadaceaeAntibacterial agentChemotherapy
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A large X-ray flare from the Herbig Ae star V892 Tau

2003

We report the XMM-Newton observation of a large X-ray flare from the Herbig Ae star V892 Tau. The apparent low mass companion of V892 Tau, V892 Tau NE, is unresolved by XMM-Newton. Nevertheless there is compelling evidence from combined XMM-Newton and Chandra data that the origin of the flare is the Herbig Ae star V892 Tau. During the flare the X-ray luminosity of V892 Tau increases by a factor of ~15, while the temperature of the plasma increases from kT ~ 1.5 keV to kT ~ 8 keV. From the scaling of the flare event, based on hydrodynamic modeling, we conclude that a 500 G magnetic field is needed in order to confine the plasma. Under the assumptions that a dynamo mechanism is required to ge…

PhysicsAstrophysics::High Energy Astrophysical PhenomenaAstrophysics (astro-ph)FOS: Physical sciencesAstronomy and AstrophysicsPlasmaAstrophysicsAstrophysics::Cosmology and Extragalactic AstrophysicsAstrophysicsMagnetic fieldLuminositylaw.inventiondisks protoplanetary disks outer diskStarsConvection zoneSpace and Planetary SciencelawAstrophysics::Solar and Stellar AstrophysicsAstrophysics::Earth and Planetary AstrophysicsLow MassAstrophysics::Galaxy AstrophysicsFlareDynamo
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Peptides Derived from the Transmembrane Domain of Bcl-2 Proteins as Potential Mitochondrial Priming Tools

2014

The Bcl-2 family of proteins is crucial for apoptosis regulation. Members of this family insert through a specific C-terminal anchoring trans membrane domain (TMD) in the mitochondrial outer membrane where they hierarchically interact to determine cell fate. While the mitochondrial membrane has been proposed to actively participate in these protein protein interactions, the influence of the TMD in the membrane-mediated interaction is poorly understood. Synthetic peptides (TMD-pepts) corresponding to the putative TMD of antiapoptotic (Bcl-2, Bcl-xL, Bcl-w, and Mcl-1) and pro-apoptotic (Bax, Bak) members were synthesized and characterized. TMD-pepts bound more efficiently to mitochondria-like…

Protein ConformationMolecular Sequence DataCell fate determinationBiochemistryHumansCell LineageAmino Acid SequenceInner mitochondrial membranebiologyChemistryCircular DichroismCytochrome cGeneral MedicineMolecular biologyMitochondriaCell biologystomatognathic diseasesTransmembrane domainMembraneProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisbiology.proteinMolecular MedicinePeptidesBacterial outer membranehuman activitiesHeLa Cells
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Immuno-electron microscopic localization of the alpha(1) and beta(1)-subunits of soluble guanylyl cyclase in the guinea pig organ of corti.

2000

Guanylyl cyclases (GC) catalyze the formation of the intracellular signal molecule cyclic GMP from GTP. For some years it has been known that the heme-containing soluble guanylyl cyclase (sGC) is stimulated by NO and NO-containing compounds. The sGC enzyme consists of two subunits (alpha(1) and beta(1)). In the present study, the alpha(1) and beta(1)-subunits were identified in the guinea pig cochlea at the electron microscopic level using a post-embedding immuno-labeling procedure. Ultrathin sections of LR White embedded specimens were incubated with various concentrations of two rabbit polyclonal antibodies to the alpha(1)- and beta(1)-subunit, respectively. The immunoreactivity was visua…

Protein subunitImmunocytochemistryGuinea PigsAntibodiesmedicineAnimalsMicroscopy ImmunoelectronMolecular BiologyHair Cells Auditory InnerbiologyTissue EmbeddingGeneral NeuroscienceMolecular biologyPrimary and secondary antibodiesHair Cells Auditory Outermedicine.anatomical_structureBiochemistrySolubilityOrgan of CortiCytoplasmGuanylate Cyclasebiology.proteinDeiters cellssense organsNeurology (clinical)Hair cellNitric Oxide SynthaseSoluble guanylyl cyclaseDevelopmental BiologySignal TransductionBrain research
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The Conservation of Low Complexity Regions in Bacterial Proteins Depends on the Pathogenicity of the Strain and Subcellular Location of the Protein

2021

Low complexity regions (LCRs) in proteins are characterized by amino acid frequencies that differ from the average. These regions evolve faster and tend to be less conserved between homologs than globular domains. They are not common in bacteria, as compared to their prevalence in eukaryotes. Studying their conservation could help provide hypotheses about their function. To obtain the appropriate evolutionary focus for this rapidly evolving feature, here we study the conservation of LCRs in bacterial strains and compare their high variability to the closeness of the strains. For this, we selected 20 taxonomically diverse bacterial species and obtained the completely sequenced proteomes of t…

Proteomics0301 basic medicinelcsh:QH426-470030106 microbiologyBiologyArticlecompositionally biased regionsEvolution MolecularLow complexity03 medical and health sciencesBacterial ProteinsSequence Analysis ProteinGeneticsExtracellularGenetics (clinical)chemistry.chemical_classificationBacteriaVirulenceStrain (chemistry)Computational Biologybiology.organism_classificationlow complexity regionsAmino acidhomorepeatslcsh:Genetics030104 developmental biologychemistryEvolutionary biologybacterial strainsProteomeorthologyBacterial outer membraneBacteriaFunction (biology)host–pathogen interactionsGenes
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Mitochondrial proteomics profile points oxidative phosphorylation as main target for beauvericin and enniatin B mixture

2020

Abstract Beauvericin (BEA) and enniatin B (EN B) are non-legislated Fusarium mycotoxins usually found in cereal and cereal-based products all around the world. By the proteomic analysis of mitochondria enriched extracts from Jurkat cells exposed for 24 h to three concentrations of BEA:EN B (0.01–0.1–0.5 μM), a number of 1821 proteins (202 mitochondrial) were identified and relatively quantified. 340 proteins (59 mitochondrial) were statistically significant altered in our samples (Anova p-value ≤ 0.05 and fold change (FC) ≥1.5). The protein mitochondrial translational release factor 1 like (MTRF1L) was the most abundant protein in the three mycotoxin exposures studied. The mycotoxins mixtur…

ProteomicsTranscription GeneticOxidative phosphorylationMitochondrionToxicologyProteomicsRibosomeJurkat cellsOxidative PhosphorylationElectron TransportMitochondrial ProteinsJurkat Cells03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyDepsipeptidesHumans030304 developmental biology0303 health sciencesfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceBeauvericinFold changeMitochondriachemistryBiochemistryBacterial outer membraneFood ScienceFood and Chemical Toxicology
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