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Active internalization of the Penicillium chrysogenum antifungal protein PAF in sensitive aspergilli

Christoph Oberparleiter1, Lydia Kaiserer, Hubertus Haas

  • 1Department of Molecular Biology, University of Innsbruck, Innsbruck, Austria.

Antimicrobial Agents and Chemotherapy
|October 25, 2003
PubMed

Insights

Penicillium chrysogenum antifungal protein PAF inhibits fungal growth. This study shows PAF enters sensitive fungi via an energy-dependent endocytotic pathway, requiring ATP and active metabolism.

Area of Science:

  • Mycology
  • Biochemistry
  • Cell Biology

Background:

  • Filamentous fungi pose significant threats to human health and agriculture.
  • Antifungal proteins offer a promising avenue for novel therapeutic strategies.
  • Penicillium chrysogenum antifungal protein (PAF) exhibits broad-spectrum antifungal activity.

Purpose of the Study:

  • To elucidate the cellular uptake mechanism of Penicillium chrysogenum antifungal protein (PAF) in sensitive fungal species.
  • To investigate the cellular localization and entry pathway of PAF.

Main Methods:

  • Indirect immunofluorescence staining was employed to visualize PAF localization within fungal cells.
  • Experiments were conducted to assess the energy dependence of PAF internalization, utilizing ATP depletion and latrunculin B treatment.

Main Results:

  • PAF was observed to localize within the cytoplasm of sensitive aspergilli.
  • The internalization of PAF was found to be an active, energy-dependent process requiring ATP.
  • Inhibition of actin polymerization by latrunculin B prevented PAF uptake, indicating a role for endocytosis.

Conclusions:

  • The antifungal protein PAF enters sensitive fungal cells through an endocytotic mechanism.
  • PAF uptake is an active, ATP-dependent process that involves cellular metabolism and cytoskeletal rearrangement.

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