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The Hsp90 Chaperone Network Modulates Candida Virulence Traits

Journal

TRENDS IN MICROBIOLOGY
Volume 25, Issue 10, Pages 809-819

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2017.05.003

Keywords

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Funding

  1. Canadian Institutes of Health Research [MOP-86452, MOP-119520]
  2. Natural Sciences and Engineering Council (NSERC) of Canada [06261, 462167]
  3. NSERC [477598]
  4. National Institutes of Health (NIH) Ruth L. Kirschstein National Research Service Award from the NIAID [AI115947-01]

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Hsp90 is a conserved molecular chaperone that facilitates the folding and function of client proteins. Hsp90 function is dynamically regulated by interactions with co-chaperones and by post-translational modifications. In the fungal pathogen Candida albicans, Hsp90 enables drug resistance and virulence by stabilizing diverse signal transducers. Here, we review studies that have unveiled regulators of Hsp90 function, as well as downstream effectors that govern the key virulence traits of morphogenesis and drug resistance. We highlight recent work mapping the Hsp90 genetic network in C. albicans under diverse environmental conditions, and how these interactions provide insight into circuitry important for drug resistance, morphogenesis, and virulence. Ultimately, elucidating the Hsp90 chaperone network will aid in the development of therapeutics to treat fungal disease.

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