0000000000389765

AUTHOR

M C Peñalver

showing 3 related works from this author

Binding of extracellular matrix proteins to Aspergillus fumigatus conidia

1996

As detected by confocal immunofluorescence microscopy, binding of fibronectin and laminin appeared to be associated with the protrusions present on the outer cell wall layer of resting Aspergillus fumigatus conidia. Flow cytometry confirmed that binding of laminin to conidia was dose dependent and saturable. Laminin binding was virtually eliminated in trypsin-treated organisms, thus suggesting the protein nature of the binding site. Conidia were also able to specifically adhere to laminin immobilized on microtiter plates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting (immunoblotting) with laminin and antilaminin antibody of whole conidial homogenates allowed…

ImmunologyMicrobiologyAspergillus fumigatusLamininCell AdhesionBinding siteCell adhesionLaminin bindingGel electrophoresischemistry.chemical_classificationExtracellular Matrix ProteinsMicroscopy ConfocalbiologyAspergillus fumigatusFlow Cytometrybiology.organism_classificationMolecular biologyFibronectinInfectious DiseasesBiochemistrychemistrybiology.proteinParasitologyGlycoproteinProtein BindingResearch ArticleInfection and Immunity
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Binding of human fibronectin to Aspergillus fumigatus conidia.

1996

Aspergillus fumigatus conidia exhibited the ability to bind purified human fibronectin, whereas mycelial forms did not bind the ligand, as detected by an indirect immunofluorescence assay with an antifibronectin polyclonal antibody after incubation of the cells with fibronectin. Flow cytometry confirmed that binding of the ligand to conidia was dose dependent and saturable. Pretreatment of the cells with trypsin markedly reduced binding, which suggested a protein nature for the binding sites present at the surface of conidia. Intact conidia were also able to adhere to fibronectin or antifibronectin antibodies, a significant reduction (from 88 to 92%) in the binding of conidia was noticed, t…

ImmunologyMicrobiologyAspergillus fumigatusFungal ProteinsMicemedicineAnimalsAspergillosisHumansTrypsinBinding siteGel electrophoresisFungal proteinbiologyAspergillus fumigatusLigand (biochemistry)biology.organism_classificationTrypsinFlow CytometryFibronectinsFibronectinInfectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinParasitologymedicine.drugResearch ArticleInfection and immunity
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Cell wall protein and glycoprotein constituents of Aspergillus fumigatus that bind to polystyrene may be responsible for the cell surface hydrophobic…

1996

Cell surface hydrophobicity (CSH) of Aspergillus fumigatus grown both in complex medium (yeast extract/peptone/dextrose; YPD) and minimal (Vogel's N) medium was monitored by assessing attachment of polystyrene microspheres to the cell surface. It was found that mature mycelium was hydrophobic. Treatment of intact mycelium with beta-mercaptoethanol (beta ME) abolished binding of the microspheres to hyphal elements, and coating of the microspheres with beta ME extracts from mycelium inhibited their attachment to intact mycelial cells. A. fumigatus mycelium was tagged in vivo with biotin and treated with beta ME. The beta ME extracts were analysed by SDS-PAGE and Western blotting with both per…

Antigens FungalMicrobiologyAspergillus fumigatusFungal ProteinsCell wallchemistry.chemical_compoundBiotinCell WallAnimalsYeast extractAntibodies FungalMyceliumchemistry.chemical_classificationMembrane GlycoproteinsbiologyAspergillus fumigatusMembrane ProteinsWaterbiology.organism_classificationMicrospheresCulture MediaMolecular WeightchemistryBiochemistryConcanavalin APolyclonal antibodiesbiology.proteinPolystyrenesRabbitsGlycoproteinMicrobiology
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