Novel Aggregation Properties of Candida albicans Secreted Aspartyl Proteinase Sap6 Mediate Virulence in Oral Candidiasis
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چکیده
منابع مشابه
A triple deletion of the secreted aspartyl proteinase genes SAP4, SAP5, and SAP6 of Candida albicans causes attenuated virulence.
Secreted aspartyl proteinases (Saps) from Candida albicans are encoded by a multigene family with at least nine members (SAP1 to SAP9) and are considered putative virulence factors important for the pathogenicity of this human pathogen. The role of Sap isoenzymes in the virulence of C. albicans has not yet been clearly established, and therefore, using recent progress in the genetics of this ye...
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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...
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A quantitative real-time RT-PCR system was established to identify which secreted aspartyl proteinase (SAP) genes are most highly expressed and potentially contribute to Candida albicans infection of human epithelium in vitro and in vivo. C. albicans SC5314 SAP1-10 gene expression was monitored in organotypic reconstituted human epithelium (RHE) models, monolayers of oral epithelial cells, and ...
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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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 2015
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.00282-15