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The Hsp90 Chaperone Network Modulates Candida Virulence Traits.
Teresa R O'Meara1, Nicole Robbins1, Leah E Cowen1
1Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5G 1M1, Canada.
Trends in Microbiology
|May 28, 2017
Summary
Heat shock protein 90 (Hsp90) is crucial for fungal pathogen Candida albicans virulence and drug resistance. Understanding its network of regulators and effectors can lead to new antifungal therapies.
Area of Science:
- Molecular biology
- Mycology
- Biochemistry
Background:
- Heat shock protein 90 (Hsp90) is a vital molecular chaperone.
- Hsp90 regulates protein folding and function, influenced by co-chaperones and post-translational modifications.
- In Candida albicans, Hsp90 is essential for drug resistance and virulence.
Purpose of the Study:
- To review studies on Hsp90 regulators and effectors in C. albicans.
- To highlight recent findings on the Hsp90 genetic network in C. albicans.
- To provide insights into Hsp90's role in fungal virulence and drug resistance.
Main Methods:
- Literature review of studies on Hsp90 function, regulation, and genetic networks.
- Analysis of Hsp90's role in C. albicans morphogenesis and drug resistance.
- Mapping of the Hsp90 genetic network under various environmental conditions.
Main Results:
- Hsp90 stabilizes key signal transducers in C. albicans.
- Regulators and downstream effectors of Hsp90 control morphogenesis and drug resistance.
- The Hsp90 genetic network in C. albicans reveals circuitry crucial for virulence.
Conclusions:
- Elucidating the Hsp90 chaperone network is key to understanding C. albicans virulence.
- Targeting the Hsp90 network offers potential for developing novel antifungal therapeutics.
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