Strain and temperature dependent aggregation of Candida auris is attenuated by inhibition of surface amyloid proteins

Dhara Malavia-Jones*, Rhys A. Farrer, Mark H.T. Stappers, Matt B. Edmondson, Andrew M. Borman, Elizabeth M. Johnson, Peter N. Lipke, Neil A.R. Gow

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


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.

Original languageEnglish
Article number100110
JournalCell Surface
Publication statusPublished - 15 Dec 2023

Bibliographical note

Funding Information:
NG acknowledges support of Wellcome Trust Investigator, Collaborative, Equipment, Strategic and Biomedical Resource awards (101873, 200208, 215599, 224323 and 200208 (the latter awarded to Daan van Aalten)) and the MRC (MR/M026663/2) and the MRC Centre for Medical Mycology (MR/N006364/2) for support. RAF is supported by a Wellcome Trust Career Development Award (225303/Z/22/Z). This study/research is also funded by the National Institute for Health and Care Research (NIHR) Exeter Biomedical Research Centre (BRC). The views expressed are those of the author(s) and not necessarily those of the NIHR or the Department of Health and Social Care.”

Publisher Copyright:
© 2023 The Authors


  • Adhesion
  • Aggregation
  • Budding
  • Cell wall
  • Medical mycology


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