Effect of antimycotic agents on the activity of aspartyl proteinases secreted by Candida albicans
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چکیده
منابع مشابه
Three distinct secreted aspartyl proteinases in Candida albicans.
The secreted aspartyl proteinases of Candida albicans (products of the SAP genes) are thought to contribute to virulence through their effects on Candida adherence, invasion, and pathogenicity. From a single strain of C. albicans (WO-1) which expresses a phenotypic switching system, three secreted aspartyl proteinases have been identified as determined by molecular weight and N-terminal sequenc...
متن کاملCandida albicans secreted aspartyl proteinases in virulence and pathogenesis.
Candida albicans is the most common fungal pathogen of humans and has developed an extensive repertoire of putative virulence mechanisms that allows successful colonization and infection of the host under suitable predisposing conditions. Extracellular proteolytic activity plays a central role in Candida pathogenicity and is produced by a family of 10 secreted aspartyl proteinases (Sap proteins...
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Objective(s): The aim of this study was to synthesize triangular gold nanoparticles, and then to evaluate their capability for inhibition of Candida albicans secreted aspartyl proteinase 2(Sap2).Materials and Methods: To synthesize the nanoparticles, hydrogen tetrachloroaurate and hexadecyl trimethyl ammonium bromide were incubated in presence of Sn(IV) meso-tetra(N-methyl-4-pyridyl) porphine t...
متن کاملSecreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells.
The endothelial cell interactions of homozygous null mutants of Candida albicans that were deficient in secreted aspartyl proteinase 1 (Sap1), Sap2, or Sap3 were investigated. Only Sap2 was found to contribute to the ability of C. albicans to damage endothelial cells and stimulate them to express E-selectin. None of the Saps studied appears to play a role in C. albicans adherence to endothelial...
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ژورنال
عنوان ژورنال: Journal of Medical Microbiology
سال: 2003
ISSN: 0022-2615,1473-5644
DOI: 10.1099/jmm.0.05048-0