Search results for "cell wall"

showing 10 items of 226 documents

Metabolism of Saccharomyces cerevisiae envelope mannoproteins.

1982

By pulse and chase labeling experiments, two independent mannoprotein pools have been found associated with the Saccharomyces cerevisiae envelope. One of them probably corresponds to mannoproteins localized in the periplasmic space. These molecules showed a high turnover rate at 28 degrees C. The second pool is formed by intrinsic wall mannoproteins which are apparently stable for long periods of time, after a small initial turnover. These results suggest that at least part of the mannoproteins initially found in the periplasmic space may move into the wall. The time lag between the addition of the radioactive precursors and their incorporation in the cell envelope (20-30 min for amino acid…

Membrane GlycoproteinsGlucan Endo-13-beta-D-GlucosidaseSaccharomyces cerevisiaeGeneral MedicineMetabolismPeriplasmic spaceSaccharomyces cerevisiaeBiologybiology.organism_classificationBiochemistryMicrobiologyYeastcarbohydrates (lipids)Cell wallFungal ProteinsMannansKineticsBiochemistryCell WallGeneticsBiophysicsMolecular BiologyEnvelope (waves)GlycoproteinsArchives of microbiology
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Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutanone: alterations in the glycoprot…

1990

Hyphal development in Candida albicans was selectively blocked by the ornithine decarboxylase competitive inhibitor 1,4-diaminobutanone (DAB). Inhibition of hyphal development required DAB during both yeast inoculum growth and subsequent incubation at 37 degrees C to induce mycelial growth. This effect was not due to general growth inhibition since DAB did not inhibit yeast growth, and reduced protein synthesis by 30% at most. Moreover, protein synthesis was unaffected by DAB when cells were pre-grown in drug-containing media. Since DAB inhibited dimorphic transition at 37 degrees C, morphology- and temperature-dependent protein synthesis could be distinguished. DAB stimulated the synthesis…

Membrane GlycoproteinsOrnithine Decarboxylase InhibitorsBiologybiology.organism_classificationMicrobiologyMolecular biologyYeastOrnithine decarboxylaseFungal Proteinschemistry.chemical_compoundchemistryBiochemistryOrnithine Decarboxylase InhibitorCell WallEnzyme inhibitorCandida albicansPutrescinebiology.proteinProtein biosynthesisGrowth inhibitionCandida albicansPolyamineJournal of General Microbiology
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Identification of a 49-kDa hydrophobic cell wall mannoprotein present in velum yeast which may be implicated in velum formation

2000

Analysis of velum-forming yeast cell wall components released by beta-1,3-glucanase treatment were compared with those of a non velum-forming yeast. SDS-PAGE electrophoresis and Western blotting with ConA-peroxidase staining of mannoproteins allowed us to identify a 49-kDa mannoprotein present in the cell wall of the velum-forming yeast and hardly visible in the control. The cell wall nature of this protein was confirmed by labelling with the non-permeable sulfosuccinimydiyl-6-(biotinamido)hexanoate reagent. A partial purification of this mannoprotein by anion exchange HPLC followed by surface hydrophobicity determination revealed that the fraction containing the 49-kDa mannoprotein was the…

Membrane GlycoproteinsSurface PropertiesBlotting WesternCellWineSaccharomyces cerevisiaeBiologyMicrobiologyYeastStainingFungal Proteinscarbohydrates (lipids)BlotCell wallElectrophoresismedicine.anatomical_structureBiochemistryCell WallBiotinylationGeneticsmedicineBiotinylationElectrophoresis Polyacrylamide GelMolecular BiologyPolyacrylamide gel electrophoresisFEMS Microbiology Letters
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Candida and Candidiasis: The Cell Wall as a Potential Molecular Target for Antifungal Therapy

2004

The fungal species Candida albicans is an opportunistic pathogen, which causes serious infections in humans, particularly in immunocompromised patients. Depending on the underlying host defect, C. albicans causes a variety of infections, ranging from superficial mucocutaneous candidiasis to life-threatening disseminated infections. Both the limited spectrum of antifungal drugs currently in clinical use and the emergence of resistances make necessary the development of new effective antifungal drugs with minimal side effects; however, such a research is limited by the small number of specific target sites identified to date. The cell wall is a fungal specific dynamic structure essential to a…

Microbiology (medical)Antifungal Agentsmedicine.medical_treatmentCellVirulenceMucocutaneous CandidiasisMicrobiologyDrug Delivery SystemsImmune systemAntigenCell WallDrug Resistance FungalmedicineHumansCandida albicansCandidaPharmacologybiologyCandidiasisImmunotherapybiology.organism_classificationCorpus albicansmedicine.anatomical_structureDrug DesignMolecular MedicineImmunotherapyCurrent Drug Target -Infectious Disorders
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Serologic Response to Cell Wall Mannoproteins and Proteins of Candida albicans

1998

SUMMARY The cell wall of Candida albicans not only is the structure in which many biological functions essential for the fungal cells reside but also is a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both the carbohydrate and protein moieties are able to trigger immune responses. Although cell-mediated immunity is often considered to be the most important line of defense against candidiasis, cell wall protein and glycoprotein components also elicit a potent humoral response from the host that may include some protective antibodies. Prot…

Microbiology (medical)Antigens FungalEpidemiologyBiologyArticleMicrobiologyFungal ProteinsImmune systemAntigenCell WallCandida albicansAnimalsHumansCandida albicanschemistry.chemical_classificationFungal proteinMembrane GlycoproteinsGeneral Immunology and MicrobiologyPublic Health Environmental and Occupational Healthbiology.organism_classificationBacterial adhesinInfectious DiseaseschemistryHumoral immunityImmunologybiology.proteinAntibodyGlycoproteinClinical Microbiology Reviews
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Antibody response toCandida albicanscell wall antigens

2003

The cell wall of Candida albicans is not only the structure where many essential biological functions reside but is also a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both carbohydrate and protein moieties are able to trigger immune responses. Proteins and glycoproteins exposed at the most external layers of the wall structure are involved in several types of interactions of fungal cells with the exocellular environment. Thus, coating of fungal cells with host antibodies has the potential to profoundly influence the host-parasite intera…

Microbiology (medical)Antigens FungalImmunologyMicrobiologyMicrobiologyImmune systemAntigenCell WallCandida albicansHumansImmunology and AllergyCandida albicansAntibodies Fungalchemistry.chemical_classificationbiologyCandidiasisGeneral Medicinebiology.organism_classificationDisseminated CandidiasisCorpus albicansBacterial adhesinInfectious DiseaseschemistryImmunologybiology.proteinAntibodyGlycoproteinFEMS Immunology & Medical Microbiology
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Diagnosis of systemic candidiasis by enzyme immunoassay detection of specific antibodies to mycelial phase cell wall and cytoplasmic candidal antigens

1993

Diagnosis of systemic Candida infections was attempted by the use of an enzyme-linked immunosorbent assay (EIA) to detect IgG antibodies towards cell wall-bound and cytoplasmic candidal antigens. Cell wall antigens were sequentially solubilized by treatment of germinated blastoconidia of Candida albicans (ATCC 26555 strain) with beta-mercaptoethanol (beta ME extract) and digestion with Zymolyase 20T, a beta-glucanase preparation (Zymolyase extract). Protoplasts obtained after treatment with Zymolyase were osmotically lysed (cytoplasmic antigens). Sera were obtained from patients with systemic (n = 28) and superficial (n = 46) candidiasis. Control sera were obtained from normal healthy indiv…

Microbiology (medical)CytoplasmAntigens FungalBlotting WesternEnzyme-Linked Immunosorbent AssaySensitivity and SpecificityBlastoconidiumMicrobiologyFungal ProteinsMannansAntigenCell WallCandida albicansmedicineHumansCandida albicansAntibodies FungalMannanMembrane Glycoproteinsbiologymedicine.diagnostic_testCandidiasisGeneral Medicinebiology.organism_classificationmedicine.diseaseCorpus albicansInfectious DiseasesImmunoglobulin GImmunoassaybiology.proteinSystemic candidiasisAntibodyLatex Fixation TestsEuropean Journal of Clinical Microbiology & Infectious Diseases
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Characterization of two Lactococcus lactis zinc membrane proteins, Llmg_0524 and Llmg_0526, and role of Llmg_0524 in cell wall integrity

2015

Background Due to its extraordinary chemical properties, the cysteine amino acid residue is often involved in protein folding, electron driving, sensing stress, and binding metals such as iron or zinc. Lactococcus lactis, a Gram-positive bacterium, houses around one hundred cysteine-rich proteins (with the CX2C motif) in the cytoplasm, but only a few in the membrane. Results In order to understand the role played by this motif we focused our work on two membrane proteins of unknown function: Llmg_0524 and Llmg_0526. Each of these proteins has two CX2C motifs separated by ten amino-acid residues (CX2CX10CX2C). Together with a short intervening gene (llmg_0525), the genes of these two protein…

Microbiology (medical)Lysozymechemistry.chemical_elementZincPlasma protein bindingGrowthMicrobiologyMembrane proteins;Growth;Cumene hydroperoxideProtein structureBacterial ProteinsCumene hydroperoxideCell Wallcystéinelactococcus lactisMembrane proteinsBenzene Derivatives[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCysteineBinding siteBinding SitesbiologyProtein StabilityLactococcus lactispropriété de membranebiology.organism_classificationcroissanceProtein Structure Tertiary3. Good healthZincchemistryBiochemistryMembrane proteinProtein foldingProtein BindingResearch ArticleCysteine
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Pathogenicity factors of mycoplasmas

1976

The pathogenicity of mycoplasmas is caused by several factors, e.g. exotoxin, toxic properties of membrane components, exoenzymes, peroxide, and immunological factors. The absence of a rigid cell wall and the small genome tend to influence the interactions between mycoplasmas and host tissue. Mycoplasmas do not have a cell wass and are therefore resistant to the action of the host's lysozymes. They appear in some patients to be immunologically inconspicuous and in other patients they have been reported to have an immuno-suppressive effect. Recently there have been reports of central nervous system disorders due to mycoplasma. The pathogenic factors involved in these reactions have not been …

Microbiology (medical)Mycoplasma pneumoniaeHost (biology)CellPathogenicity FactorsGeneral MedicineMycoplasmaBiologymedicine.disease_causeGenomeVirologyMicrobiologyCell wallMycoplasmaInfectious Diseasesmedicine.anatomical_structuremedicineAnimalsHumansExotoxinToxins BiologicalInfection
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Yarrowia lipolytica cell wall architecture: interaction of Ywp1, a mycelial protein, with other wall components and the effect of its depletion

1999

Linkages of Ywp1 to other components of the Yarrowia lipolytica mycelial cell wall were studied by extraction with beta-mercaptoethanol and zymolyase (a beta-glucanase complex) and by the use of rabbit polyclonal antibody preparation raised against Ywp1. Ywp1 complexed with an N-glycosylated cell wall protein(s) to form supramolecular complexes through disulphide bridges (extractable with beta-mercaptoethanol) or bonded to beta-1,3-glucan (extractable with zymolyase). The lack of a specific morphological phenotype when YWP1 was knocked out by gene disruption might indicate that other proteins present in the cell wall of Y. lipolytica compensated for its loss. In this mutant, the electrophor…

Microscopy ConfocalbiologyBlotting WesternMutantYarrowiaGeneral MedicineCalcofluor-whitebiology.organism_classificationMicrobiologyWheat germ agglutininFungal ProteinsCell wallchemistry.chemical_compoundPhenotypeBiochemistryChitinchemistryCell WallPolyclonal antibodiesSaccharomycetalesChitinasebiology.proteinAnimalsRabbitsMolecular BiologyResearch in Microbiology
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