Search results for "Fibronectin binding"

showing 4 items of 4 documents

Fibronectin-binding nanoparticles for intracellular targeting addressed by B. burgdorferi BBK32 protein fragments.

2011

Virus-like particles (VLPs) are created by the self-assembly of multiple copies of envelope and/or capsid proteins from many viruses, mimicking the conformation of a native virus. Such noninfectious nanostructures are mainly used as antigen-presenting platforms, especially in vaccine research; however, some of them recently were used as scaffolds in biotechnology to produce targeted nanoparticles for intracellular delivery. This study demonstrates the creation of fusion VLPs using hepatitis B core protein-based system maintaining a fibronectin-binding property from B. burgdorferi BBK32 protein, including the evidence of particles’ transmission to BHK-21 target cells via caveolae/rafts endoc…

:MEDICINE [Research Subject Categories]virusesBiomedical EngineeringPharmaceutical ScienceMedicine (miscellaneous)BioengineeringPeptideBiologyVirusPlasmidBacterial ProteinsCaveolaeGeneral Materials ScienceDNA Primerschemistry.chemical_classificationBase SequenceVirologyCell biologyFibronectins:NATURAL SCIENCES::Biology [Research Subject Categories]FibronectinchemistryCapsidFibronectin bindingBorrelia burgdorferibiology.proteinMolecular MedicineNanoparticlesIntracellularPlasmidsNanomedicine : nanotechnology, biology, and medicine
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The hemagglutinin of Staphylococcus saprophyticus binds to a protein receptor on sheep erythrocytes.

1997

Staphylococcus saprophyticus, an important cause of urinary tract infections, produces two major surface proteins, the S. saprophyticus surface-associated protein (Ssp) and the hemagglutinin, which mediates fibronectin binding and also functions as the major adhesion of the organism. The hemagglutinating and fibronectin binding functions probably reside on different parts of the molecule. To identify a receptor on eukaryotic cells, binding and inhibition studies with acidic and neutral glycosphingolipids, carbohydrates, and proteins of sheep erythrocyte membranes were conducted. S. saprophyticus did not bind to any glycosphingolipid and no inhibition was observed when hemagglutination assay…

Microbiology (medical)HemagglutinationStaphylococcusImmunologyBiologyBacterial AdhesionGlycosphingolipidsMicrobiologyImmunology and AllergyAnimalsHumanschemistry.chemical_classificationStaphylococcus saprophyticusSheepHemagglutinationErythrocyte MembraneMembrane ProteinsGeneral MedicineBlood ProteinsHemagglutininLigand (biochemistry)biology.organism_classificationMolecular WeightBiochemistryMembrane proteinchemistryFibronectin bindingGalactose oxidaseGlycoproteinMedical microbiology and immunology
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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
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Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase fromCandida albicans

1999

We report here the purification of a functionally active recombinant glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from Candida albicans. The GAPDH protein encoded by the TDH1 gene was obtained as a glutathione S-transferase fusion protein by expression in the vector pGEX-4T-3, and purified by affinity chromatography and thrombin digestion. The purified protein displays GAPDH enzymatic activity (42 micromol NADH min(-1) mg(-1)) as well as the laminin and fibronectin binding activities previously described. In addition, the recombinant GAPDH is covalently modified by NAD linkage; this modification is stimulated by nitric oxide and probably involves a sulfhydryl group (cysteine) residue si…

Recombinant Fusion ProteinsDehydrogenaseBiologyMicrobiologyChromatography Affinitylaw.inventionchemistry.chemical_compoundstomatognathic systemAffinity chromatographylawGlyceraldehydeCandida albicansEscherichia coliGeneticsCloning MolecularMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseGlutathione TransferaseThrombinGlyceraldehyde-3-Phosphate DehydrogenasesMolecular biologyRecombinant ProteinsKineticschemistryBiochemistryFibronectin bindingbiology.proteinRecombinant DNAGlyceraldehyde 3-phosphateCysteineFEMS Microbiology Letters
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