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• W4385216504 startingPage "100110" @default.
• W4385216504 abstract "Candida auris is a multi-drug resistant human fungal pathogen that has become a global threat to human health due to its drug resistant phenotype, persistence in the hospital environment and propensity for patient to patient spread. Isolates display variable aggregation that may affect the relative virulence of strains. Therefore, dissection of this phenotype has gained substantial interest in recent years. We studied eight clinical isolates from four different clades (I-IV); four of which had a strongly aggregating phenotype and four of which did not. Genome analysis identified polymorphisms associated with loss of cell surface proteins were enriched in weakly-aggregating strains. Additionally, we identified down-regulation of chitin synthase genes involved in the synthesis of the chitinous septum. Characterisation of the cells revealed no ultrastructural defects in cytokinesis or cell separation in aggregating isolates. Strongly and weakly aggregating strains did not differ in net surface charge or in cell surface hydrophobicity. The capacity for aggregation and for adhesion to polystyrene microspheres were also not correlated. However, aggregation and extracellular matrix formation were all increased at higher growth temperatures, and treatment with the amyloid protein inhibitor Thioflavin-T markedly attenuated aggregation. Genome analysis further indicated strain specific differences in the genome content of GPI-anchored proteins including those encoding genes with the potential to form amyloid proteins. Collectively our data suggests that aggregation is a complex strain and temperature dependent phenomenon that may be linked in part to the ability to form extracellular matrix and cell surface amyloids." @default.
• W4385216504 created "2023-07-25" @default.
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• W4385216504 date "2023-12-01" @default.
• W4385216504 modified "2023-10-14" @default.
• W4385216504 title "Strain and temperature dependent aggregation of Candida auris is attenuated by inhibition of surface amyloid proteins" @default.
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• W4385216504 doi "https://doi.org/10.1016/j.tcsw.2023.100110" @default.
• W4385216504 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37559873" @default.
• W4385216504 hasPublicationYear "2023" @default.
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