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Antimicrobial Agents and Chemotherapy, June 2005, p. 2445-2453, Vol. 49, No. 6
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.6.2445-2453.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Antifungal Protein PAF Severely Affects the Integrity of the Plasma Membrane of Aspergillus nidulans and Induces an Apoptosis-Like Phenotype

Éva Leiter,1 Henrietta Szappanos,2 Christoph Oberparleiter,3 Lydia Kaiserer,3 László Csernoch,2 Tünde Pusztahelyi,1 Tamás Emri,1 István Pócsi,1 Willibald Salvenmoser,4 and Florentine Marx3*

Department of Microbiology and Biotechnology, Faculty of Science,1 Department of Physiology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Debrecen, Hungary,2 Biocenter, Division of Molecular Biology, Innsbruck Medical University, Innsbruck, Austria,3 Institute of Zoology and Limnology, Division of Ultrastructure and Evolutionary Biology, University of Innsbruck, Innsbruck, Austria4

Received 20 August 2004/ Returned for modification 24 August 2004/ Accepted 9 February 2005

The small, basic, and cysteine-rich antifungal protein PAF is abundantly secreted into the supernatant by the ß-lactam producer Penicillium chrysogenum. PAF inhibits the growth of various important plant and zoopathogenic filamentous fungi. Previous studies revealed the active internalization of the antifungal protein and the induction of multifactorial detrimental effects, which finally resulted in morphological changes and growth inhibition in target fungi. In the present study, we offer detailed insights into the mechanism of action of PAF and give evidence for the induction of a programmed cell death-like phenotype. We proved the hyperpolarization of the plasma membrane in PAF-treated Aspergillus nidulans hyphae by using the aminonaphtylethenylpyridinium dye di-8-ANEPPS. The exposure of phosphatidylserine on the surface of A. nidulans protoplasts by Annexin V staining and the detection of DNA strand breaks by TUNEL (terminal deoxynucleotidyltransferase-mediated dUTP-biotin nick end labeling) gave evidence for a PAF-induced apoptotic-like mechanism in A. nidulans. The localization of reactive oxygen species (ROS) by dichlorodihydrofluorescein diacetate and the abnormal cellular ultrastructure analyzed by transmission electron microscopy suggested that ROS-elicited membrane damage and the disintegration of mitochondria played a major role in the cytotoxicity of PAF. Finally, the reduced PAF sensitivity of A. nidulans strain FGSC1053, which carries a dominant-interfering mutation in fadA, supported our assumption that G-protein signaling was involved in PAF-mediated toxicity.

* Corresponding author. Mailing address: Biocenter, Division of Molecular Biology, Innsbruck Medical University, Fritz-Pregl Strasse 3, A-6020 Innsbruck, Austria. Phone: 43-512-5073607. Fax: 43-512-5079880. E-mail: florentine.marx{at}uibk.ac.at.

Antimicrobial Agents and Chemotherapy, June 2005, p. 2445-2453, Vol. 49, No. 6
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.6.2445-2453.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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