The trimorphic fungus Candida albicans is the leading cause of systemic candidiasis, a disease with poor prognosis affecting immunocompromised patients. The capacity to switch between growth morphologies is tightly coupled to its ability to cause life-threatening infection. Recently, the molecular chaperone Heat Shock Protein 90 (Hsp90) has been implicated as a major regulator of C. albicans morphogenesis via the Ras1-PKA pathway. In model organisms from plant, animal and fungal kingdoms, Hsp90 stabilizes regulators of cell signaling and participates in many important cellular processes. Hsp90’s roles in C. albicans are beginning to be dissected. This thesis represents a comprehensive overview of the morphological response of C. albicans to compromised Hsp90 function, illuminating previously unidentified roles for this chaperone in cell cycle progression, cytokinesis and vacuole maintenance. This work sheds light on the importance of Hsp90 in fungal development and the therapeutic potential of Hsp90 inhibitors in the treatment of fungal infections.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:OTU.1807/33705 |
| Date | 03 December 2012 |
| Creators | Senn, Heather |
| Contributors | Cowen, Leah |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | en_ca |
| Detected Language | English |
| Type | Thesis |
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