Search results for "Outer membrane protein"

showing 10 items of 52 documents

Expression of Staphylococcus saprophyticus surface properties is modulated by composition of the atmosphere.

1995

Expression of two major surface proteins of Staphylococcus saprophyticus, the haemagglutinin and the Staphylococcus saprophyticus surface-associated protein (Ssp), requires carefully defined culture conditions. The Ssp is produced when bacteria are grown on agar, whereas expression of the haemagglutinin requires growth in broth. We sought to identify the environmental signals that are responsible for this modulation. Varying the pH, the osmolarity of the growth medium or the temperature did not influence expression of the proteins. In contrast, growth in an anaerobic atmosphere increased haemagglutination titres and fibronectin binding (both mediated by the haemagglutinin) but suppressed pr…

Microbiology (medical)food.ingredientStaphylococcusImmunologyBiologyMicrobiologychemistry.chemical_compoundfoodBacterial ProteinsImmunology and AllergyAgarAdhesins Bacterialchemistry.chemical_classificationGrowth mediumStaphylococcus saprophyticusOsmotic concentrationGeneral MedicineHemagglutininbiology.organism_classificationFibronectinsMolecular WeightHemagglutininsFibronectin bindingchemistryBiochemistryGlycoproteinCarrier ProteinsBacteriaBacterial Outer Membrane ProteinsMedical microbiology and immunology
researchProduct

Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi

2014

Borrelia burgdorferi, the causative agent of Lyme disease is transmitted to the mammalian host organisms by infected Ixodes ticks. Transfer of the spirochaetal bacteria from Ixodes ticks to the warm-blooded mammalian organism provides a challenge for the bacteria to adapt and survive in the different environmental conditions. B. burgdorferi has managed to differentially express genes in response to the encountered changes such as temperature and pH variance or metabolic rate to survive in both environments. In recent years, much interest has been turned on genes that are upregulated during the borrelial transfer to mammalian organisms as this could reveal the proteins important in the patho…

Models MolecularMolecular Sequence DataSequence alignmentCrystallography X-RayMicrobiologyMicrobiologyLyme diseasemedicineAnimalsAmino Acid SequenceBorrelia burgdorferiGeneAntigens BacterialLyme DiseaseIxodesbiologyProtein superfamilybiology.organism_classificationmedicine.diseasePhenotypeInfectious DiseasesMembrane proteinBorrelia burgdorferiInsect ScienceParasitologyIxodesSequence AlignmentBacterial Outer Membrane ProteinsTicks and Tick-borne Diseases
researchProduct

Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism.

2013

Borrelia burgdorferi, which is the causative agent of Lyme disease, is transmitted from infected Ixodes ticks to a mammalian host following a tick bite. Upon changing the host organism from an Ixodes tick to a warm-blooded mammal, the spirochete must adapt to very different conditions, which is achieved by altering the expression of several genes in response to a changing environment. Recently, considerable attention has been devoted to several outer surface proteins, including BBA73, that undergo dramatic upregulation during the transmission of B. burgdorferi from infected Ixodes ticks to mammals and that are thought to be important for the establishment and maintenance of the infection. T…

Models MolecularMolecular Sequence DataStatic ElectricityBiophysicsCrystallography X-RayBiochemistryProtein Structure SecondaryMicrobiologyProtein structureAnimalsAmino Acid SequenceBorrelia burgdorferiCloning MolecularProtein Structure QuaternaryMolecular BiologyPeptide sequenceLyme DiseaseBinding SitesbiologyIxodesSequence Homology Amino AcidCell BiologyProtein superfamilyLigand (biochemistry)biology.organism_classificationSolutionsMembrane proteinBorrelia burgdorferiLyme disease microbiologyIxodesProtein MultimerizationBacterial Outer Membrane ProteinsBiochemical and biophysical research communications
researchProduct

Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

2020

Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of Borrelia tunicate outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family. This article is protected …

Models MolecularProtein Conformation alpha-HelicalProtein familyLipoproteinsGenetic VectorsGene ExpressionPeptideBiochemistryMicrobiologyPathogenesis03 medical and health sciencesLyme diseaseStructural BiologyBorreliamedicineEscherichia coliHumansProtein Interaction Domains and MotifsAmino Acid SequenceBorrelia burgdorferiCloning MolecularMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseasebiologySequence Homology Amino AcidBorrelia030302 biochemistry & molecular biologybacterial infections and mycosesbiology.organism_classificationmedicine.diseaseRecombinant ProteinsProtein Structure TertiaryOuter surface proteinchemistryBorrelia burgdorferiProtein Conformation beta-StrandSequence AlignmentLipoproteinBacterial Outer Membrane ProteinsProteinsREFERENCES
researchProduct

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
researchProduct

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
researchProduct

Immunogenic antigens of the eel pathogen Vibrio vulnificus serovar E.

2003

Abstract The immunogenic antigens of Vibrio vulnificus serovar E were investigated in the eel. Fish were vaccinated by immersion with Vulnivaccine (V), revaccinated 2 years later by intraperitoneal injection (RV) and bath infected 15 days post-revaccination (RVI). The specific immune response in serum was followed in all groups, and selected sera were used for immunostaining of surface (SA) and extracellular antigens (ECA). Bacteria were grown in iron-rich (TSB and MSWYE) and iron-poor media (TSB and MSWYE plus human transferrin (TSB-T and MSWYE-T)) as well as eel serum (ES), and their SA and ECA were extracted and electrophoretically analysed. Cells grown in MSWYE-T and ES presented the sa…

SerotypeLipopolysaccharidesTime FactorsLipopolysaccharideIronImmunoblottingEnzyme-Linked Immunosorbent AssayVibrio vulnificusAquatic ScienceMicrobiologychemistry.chemical_compoundAntigenEnvironmental ChemistryAnimalsPathogenVibrio vulnificuschemistry.chemical_classificationAntigens BacterialbiologyImmune SeraGeneral Medicinebiology.organism_classificationAnguillachemistryTransferrinAntibody FormationBacterial VaccinesElectrophoresis Polyacrylamide GelBacterial outer membraneBacteriaBacterial Outer Membrane ProteinsFishshellfish immunology
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct