Search results for "Bacterial Outer Membrane Proteins"

showing 10 items of 50 documents

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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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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IMMUNOGENICITY OF AN ACELLULAR PERTUSSIS VACCINE COMPOSED OF GENETICALLY INACTIVATED PERTUSSIS TOXIN COMBINED WITH FILAMENTOUS HEMAGGLUTININ AND PERT…

1993

We studied the immunogenicity of an acellular pertussis vaccine composed of genetically detoxified pertussis toxin (PT-9K/129G), filamentous haemagglutinin, and a 69-kilodalton protein, pertactin, in 30 children aged 12 to 24 months and in 80 infants aged 2 to 4 months. A significant increase of the neutralizing titer and of the titers against pertussis toxin, filamentous hemagglutinin, and pertactin, as determined by enzyme-linked immunosorbent assay, was achieved after three doses of vaccine in all the children; a significant increase of these antibody titers was obtained in 100%, 96.1%, 93.5%, and 98.7% of the infants, respectively.

Time FactorsFilamentous haemagglutinin adhesinPertussis toxincomplex mixturesBordetella pertussisMicrobiologyNeutralization TestsHumansMedicineVirulence Factors BordetellaAdhesins BacterialImmunization ScheduleWhooping coughPertussis VaccineAntigens Bacterialbusiness.industryImmunogenicitypertussisAntibody titerInfantmedicine.diseaseAntibodies BacterialVirologyVaccinationTiterHemagglutininsPertussis ToxinVaccines InactivatedChild PreschoolImmunoglobulin GPediatrics Perinatology and Child HealthDrug EvaluationPertactinbusinessVaccinepertussis; VaccineBacterial Outer Membrane Proteins
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Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2.

2000

ABSTRACT Attaching and effacing (A/E) rabbit enteropathogenic Escherichia coli (REPEC) strains belonging to serogroup O103 are an important cause of diarrhea in weaned rabbits. Like human EPEC strains, they possess the locus of enterocyte effacement clustering the genes involved in the formation of the A/E lesions. In addition, pathogenic REPEC O103 strains produce an Esp-dependent but Eae (intimin)-independent alteration of the host cell cytoskeleton characterized by the formation of focal adhesion complexes and the reorganization of the actin cytoskeleton into bundles of stress fibers. To investigate the role of intimin and its translocated coreceptor (Tir) in the pathogenicity of REPEC, …

Time Factors[SDV]Life Sciences [q-bio]MutantAdministration OralPATHOGENICITEmedicine.disease_causeBacterial AdhesionMICROSCOPIE ELECTRONIQUE A TRANSMISSIONFecesCytoskeleton0303 health sciencesVirulenceEscherichia coli ProteinsEnterobacteriaceae3. Good health[SDV] Life Sciences [q-bio]IntestinesInfectious DiseasesMolecular and Cellular PathogenesisRabbitsLocus of enterocyte effacementBacterial Outer Membrane ProteinsImmunologyMolecular Sequence DataVirulenceReceptors Cell SurfaceBiologyMicrobiologydigestive systemMicrobiologyCell Line03 medical and health sciencesBacterial ProteinsIleummedicineEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliAdhesins BacterialEscherichia coli030304 developmental biologyIntiminModels Genetic030306 microbiologyGenetic Complementation TestEpithelial Cellsbiochemical phenomena metabolism and nutritionbiology.organism_classificationActin cytoskeleton[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyActinsKineticsMicroscopy ElectronMicroscopy FluorescenceMutagenesisParasitologyCarrier ProteinsHeLa CellsInfection and immunity
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The yopJ locus is required for Yersinia-mediated inhibition of NF-kappaB activation and cytokine expression: YopJ contains a eukaryotic SH2-like doma…

1998

Upon exposure to bacteria, eukaryotic cells activate signalling pathways that result in the increased expression of several defence-related genes. Here, we report that the yopJ locus of the enteropathogen Yersinia pseudotuberculosis encodes a protein that inhibits the activation of NF-kappaB transcription factors by a mechanism(s), which prevents the phosphorylation and subsequent degradation of the inhibitor protein IkappaB. Consequently, eukaryotic cells infected with YopJ-expressing Yersinia become impaired in NF-kappaB-dependent cytokine expression. In addition, the blockage of inducible cytokine production coincides with yopJ-dependent induction of apoptosis. Interestingly, the YopJ pr…

Transcriptional Activationmedicine.medical_treatmentMolecular Sequence DataApoptosisBiologySH2 domainTransfectionMicrobiologysrc Homology DomainsGenes ReportermedicineYersinia pseudotuberculosisHumansAmino Acid SequenceMolecular BiologyGeneTranscription factorCells CulturedSrc homology domainVirulenceTumor Necrosis Factor-alphaMacrophagesNF-kappa BYersiniosisGene Expression Regulation Bacterialbiology.organism_classificationmedicine.diseaseFlow CytometryMolecular biologyCell biologyCytokineYersinia pseudotuberculosisPhosphorylationCytokinesBacterial Outer Membrane ProteinsHeLa CellsPlasmidsMolecular microbiology
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Insertion of a malE B-Galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processin…

1982

The synthesis of a membrane-bound MalE ,B-galactosidase hybrid protein, when induced by growth of Escherichia coli on maltose, leads to inhibition of cell division and eventually a reduced rate of mass increase. In addition, the relative rate of synthesis of outer membrane proteins, but not that of inner membrane proteins, was reduced by about 50%o. Kinetic experiments demonstrated that this reduction coincided with the period of maximum synthesis of the hybrid protein (and another maltose-inducible protein, LamB). The accumulation of this abnormal protein in the envelope therefore appeared specifically to inhibit the synthesis, the assembly of outer membrane proteins, or both, indicating t…

Vesicle-associated membrane protein 8MembranesPeripheral membrane proteinDNA RecombinantMembrane ProteinsPorinsBiologyMicrobiologyCell biologyTransport proteinKineticsEscheríchia coliBacterial ProteinsMembrane proteinEscherichia coliReceptors VirusOuter membrane efflux proteinsInner membraneProtein PrecursorsMaltoseBacterial outer membraneMolecular BiologyIntegral membrane proteinProteïnesBacterial Outer Membrane Proteins
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Serological and molecular characteristics of Vibrio vulnificus biotype 3: evidence for high clonality.

2007

Vibrio vulnificus biotype 3 has been implicated as the causative pathogen of an ongoing disease outbreak that erupted in Israel in 1996. Recent work based on multi-locus sequence typing (MLST) showed that V. vulnificus biotype 3 is genetically homogeneous. The aim of this study was to investigate the existence of subpopulations within this homogeneous biotype by characterizing the surface antigens and analysing the sequence diversity of selected outer-membrane protein (OMP)-encoding genes. Rabbit antisera were prepared against biotype 1, 2 and 3 strains. The results of the slide-agglutination test, dot-blot assay (using fresh and boiled cells), and immunoblotting of lipopolysaccharides (LPS…

clone (Java method)DNA BacterialLipopolysaccharidesPopulationImmunoblottingMolecular Sequence DataSequence HomologyBiologyMicrobiologyDNA sequencingMicrobiologyEvolution MolecularAgglutination TestsCluster AnalysisHumansTypingIsraeleducationGenePathogenVibrio vulnificuseducation.field_of_studyAntigens BacterialMolecular EpidemiologyBase SequenceStrain (biology)Genetic Variationbacterial infections and mycosesVibrio InfectionsbacteriaMultilocus sequence typingBacterial Outer Membrane ProteinsMicrobiology (Reading, England)
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Studies on the interaction of C1q,a subcomponent of the first component of complement, with porins fromSalmonella minnesotaincorporated into artifici…

1990

AbstractPurified outer membrane proteins (OMP) of Salmonella minnesota, Re-form, were incorporated into liposomes. These induced in macrophages a chemiluminescence signal identical to that of the intact Re-form. This signal was abolished by preincubation of porin-containing liposomes with purified C1q. Incorporation of isolated OMP into black lipid membranes (BLM) resulted in channel-formation which could not be inhibited by isolated C1q. Additionally, incubation of OMP-containing liposomes with BLM resulted in pore-formation within the BLM. This was amplified when lipid A was present within the liposomes. Preincubation of OMP-containing liposomes with purified C1q abolished pore-formation …

congenital hereditary and neonatal diseases and abnormalitiesLuminescenceMacrophageLipid BilayersBiophysicsSynthetic membranePorinschemical and pharmacologic phenomenaBiochemistryIon ChannelsMembrane PotentialsLipid AMiceSalmonellaStructural BiologyGeneticsAnimalsHumansBlack lipid membraneLipid bilayerMolecular BiologyC1qCells CulturedMice Inbred BALB CLiposomeurogenital systemChemistryComplement C1qMacrophagesElectric Conductivitynutritional and metabolic diseasesMembranes ArtificialCell BiologyLiposomeKineticsCholesterolMembraneMembrane proteinBiochemistryOuter membrane proteinPorinPhosphatidylcholinesbacteriaBacterial outer membraneBacterial Outer Membrane ProteinsFEBS Letters
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The Efflux Pump MexXY/OprM Contributes to the Tolerance and Acquired Resistance of Pseudomonas aeruginosa to Colistin

2020

The intrinsic resistance of Pseudomonas aeruginosa to polymyxins in part relies on the addition of 4-amino-4-deoxy-l-arabinose (Ara4N) molecules to the lipid A of lipopolysaccharide (LPS), through induction of operon arnBCADTEF-ugd (arn) expression. As demonstrated previously, at least three two-component regulatory systems (PmrAB, ParRS, and CprRS) are able to upregulate this operon when bacteria are exposed to colistin. In the present study, gene deletion experiments with the bioluminescent strain PAO1::lux showed that ParRS is a key element in the tolerance of P. aeruginosa to this last-resort antibiotic (i.e., resistance to early drug killing). Other loci of the ParR regulon, such as th…

medicine.drug_classOperonPolymyxinMutantMicrobial Sensitivity Testsmedicine.disease_causeMicrobiologyLipid A03 medical and health sciencesBacterial ProteinsMechanisms of ResistanceDrug Resistance BacterialmedicinePharmacology (medical)ComputingMilieux_MISCELLANEOUS030304 developmental biologyPharmacology0303 health sciencesColistin030306 microbiologyPseudomonas aeruginosaChemistryMembrane Transport ProteinsGene Expression Regulation BacterialAnti-Bacterial AgentsInfectious DiseasesRegulonPseudomonas aeruginosa[SDE]Environmental SciencesColistinlipids (amino acids peptides and proteins)EffluxGene DeletionBacterial Outer Membrane Proteinsmedicine.drugAntimicrobial Agents and Chemotherapy
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A novel intrinsically disordered outer membrane lipoprotein ofAggregatibacter actinomycetemcomitansbinds various cytokines and plays a role in biofil…

2017

Intrinsically disordered proteins (IDPs) do not have a well-defined and stable 3-dimensional fold. Some IDPs can function as either transient or permanent binders of other proteins and may interact with an array of ligands by adopting different conformations. A novel outer membrane lipoprotein, bacterial interleukin receptor I (BilRI) of the opportunistic oral pathogen Aggregatibacter actinomycetemcomitans binds a key gatekeeper proinflammatory cytokine interleukin (IL)-1b. Because the amino acid sequence of the novel lipoprotein resembles that of fibrinogen binder A of Haemophilus ducreyi, BilRI could have the potential to bind other proteins, such as host matrix proteins. However, from th…

outer membrane lipoproteinsbacterial cytokine receptorbiofilm matrix composition0301 basic medicineMicrobiology (medical)Virulence FactorsLipoproteinsInterleukin-1beta030106 microbiologyImmunologyGingivaBiologyIntrinsically disordered proteinsAggregatibacter actinomycetemcomitansMicrobiologybacterial cytokine receptors03 medical and health sciencesHumansInterleukin 8Periodontal Diseasesouter membrane lipoproteinTumor Necrosis Factor-alphaInterleukin-8ta1182Biochemistry and Molecular BiologyBiofilmAggregatibacter actinomycetemcomitansReceptors Interleukin-1food and beveragesintrinsically disordered proteinbiology.organism_classificationInterleukin-10Cell biologyIntrinsically Disordered ProteinsInterleukin 10EditorialInfectious DiseasesBiochemistryBiofilmsParasitologyTumor necrosis factor alphabiofilm matrix compositionsintrinsically disordered proteinsBacterial outer membraneBiokemi och molekylärbiologiResearch PaperBacterial Outer Membrane ProteinsLipoproteinVirulence
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