0000000000116637

AUTHOR

Christine Schindel

showing 3 related works from this author

PKSP-dependent reduction of phagolysosome fusion and intracellular kill of Aspergillus fumigatus conidia by human monocyte-derived macrophages.

2002

Summary Previously, we described the isolation of an Aspergillus fumigatus mutant producing non-pigmented conidia, as a result of a defective polyketide synthase gene, pksP (polyketide synthase involved in pigment biosynthesis). The virulence of the pksP mutant was attenuated in a murine animal infection model and its conidia showed enhanced susceptibility towards damage by monocytes in vitro. Because macrophage-mediated killing is critical for host resistance to aspergillosis, the interaction of both grey-green wild-type conidia and white pksP mutant conidia with human monocyte-derived macrophages (MDM) was studied with respect to intracellular processing of ingested conidia. After phagocy…

PhagocytosisImmunologyMutantVirulenceMicrobiologyPhagolysosomeMonocytesMicrobiologyAspergillus fumigatusConidiumCell FusionPhagocytosisMultienzyme ComplexesVirologyPhagosomesAspergillosisHumansskin and connective tissue diseasesCells CulturedPhagosomebiologyAspergillus fumigatusMacrophagesfungirespiratory systembiology.organism_classificationAcridine OrangeIntracellularCellular microbiology
researchProduct

Early detection of Toxoplasma infection by molecular monitoring of Toxoplasma gondii in peripheral blood samples after allogeneic stem cell transplan…

2004

International audience; Background. Isolated case reports have shown that recipients of allogeneic hematopoietic stem cell transplants ( HSCTs) who develop toxoplasmosis may have circulating Toxoplasma gondii DNA in peripheral blood before the onset of clinical symptoms. Methods. We prospectively studied 106 T. gondii - seropositive adult recipients of HSCTs for the incidence of reactivation of toxoplasmosis in the first 6 months after transplantation. Toxoplasmosis infection ( TI) was defined by a positive result of polymerase chain reaction ( PCR) of peripheral blood specimens, whereas toxoplasmosis disease ( TD) was defined as an invasive infection. Results. The incidence of TI was 16% (…

AdultMicrobiology (medical)POLYMERASE-CHAIN-REACTIONmedicine.medical_treatment[SDV]Life Sciences [q-bio]Hematopoietic stem cell transplantationPolymerase Chain ReactionParasite loadCYTOMEGALOVIRUS-INFECTIONBlood cell03 medical and health sciencesIMMUNE RECONSTITUTION0302 clinical medicinemedicineAnimalsHumansTransplantation Homologous030212 general & internal medicineREAL-TIME PCR0303 health sciencesHematologic Testsbiology030306 microbiologybusiness.industryIncidence (epidemiology)Toxoplasma gondiiDNA Protozoanbiology.organism_classificationmedicine.diseaseBONE-MARROW-TRANSPLANTATIONPREEMPTIVE THERAPYToxoplasmosis3. Good healthTransplantationRECIPIENTSInfectious DiseasesReal-time polymerase chain reactionmedicine.anatomical_structureImmunologySTATISTICAL-METHODSTRANSFER HYBRIDIZATION PROBESbusinessToxoplasmaToxoplasmosisStem Cell Transplantation
researchProduct

Interaction ofEscherichia colihemolysin with biological membranes

2001

Escherichia coli hemolysin (HlyA) is a membrane-permeabilizing protein belonging to the family of RTX-toxins. Lytic activity depends on binding of Ca2(+) to the C-terminus of the molecule. The N-terminus of HlyA harbors hydrophobic sequences that are believed to constitute the membrane-inserting domain. In this study, 13 HlyA cysteine-replacement mutants were constructed and labeled with the polarity-sensitive fluorescent probe 6-bromoacetyl-2-dimethylaminonaphthalene (badan). The fluorescence emission of the label was examined in soluble and membrane-bound toxin. Binding effected a major blue shift in the emission of six residues within the N-terminal hydrophobic domain, indicating inserti…

Conformational changeProtein ConformationPlasma protein bindingBiologymedicine.disease_causeHemolysisBiochemistryHemolysin ProteinsProtein structureBacterial Proteins2-NaphthylamineEscherichia colimedicineCysteineCloning MolecularLipid bilayerEscherichia coliFluorescent DyesEscherichia coli ProteinsCell MembraneErythrocyte MembraneBiological membraneProtein Structure TertiarySpectrometry FluorescenceMembraneBiochemistryMutagenesisLiposomesChromatography GelCalciumElectrophoresis Polyacrylamide GelProtein BindingBinding domainEuropean Journal of Biochemistry
researchProduct