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Heat shock protein 90 is required for conidiation and cell wall integrity in Aspergillus fumigatus

Frédéric Lamoth1, Praveen R Juvvadi, Jarrod R Fortwendel

  • 1Division of Pediatric Infectious Diseases, Department of Pediatrics, Duke University Medical Center, Durham, NC, USA.

Eukaryotic Cell
|July 24, 2012
PubMed

Insights

Heat shock protein 90 (Hsp90) is essential for Aspergillus fumigatus growth and development. Inhibiting Hsp90 enhances antifungal drug efficacy and reveals its role in cell wall integrity and stress responses.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Mycology

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone in eukaryotes.
  • Hsp90's role in antifungal resistance is known for Candida albicans but not Aspergillus fumigatus.

Purpose of the Study:

  • To investigate the function of Hsp90 in the filamentous fungus Aspergillus fumigatus.
  • To explore Hsp90's cellular localization under stress and its impact on antifungal drug efficacy.

Main Methods:

  • Genetic repression of Hsp90 using an inducible promoter (pniiA-Hsp90).
  • Assessing effects on spore viability, hyphal growth, germination, and conidiation.
  • Investigating Hsp90 localization via GFP tagging under various stress conditions.
  • Evaluating the impact of Hsp90 inhibition on cell wall integrity and antifungal drug response.

Main Results:

  • Hsp90 is essential for A. fumigatus viability, growth, and development.
  • Hsp90 repression led to defects in germination, conidiation, and downregulation of key transcription factors.
  • Hsp90 inhibition potentiated caspofungin and FK506 effects, indicating a role in cell wall integrity.
  • Hsp90 localized to the cell wall and septa upon caspofungin treatment, suggesting stress response involvement.

Conclusions:

  • Hsp90 plays a vital role in A. fumigatus cell wall integrity and stress adaptation.
  • Targeting Hsp90 offers a promising strategy for developing new antifungal therapies against A. fumigatus.

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