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J. Biol. Chem., Vol. 282, Issue 26, 18831-18841, June 29, 2007

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Energy Depletion Protects Candida albicans against Antimicrobial Peptides by Rigidifying Its Cell Membrane^*

Enno C. I. Veerman¹, Marianne Valentijn-Benz, Kamran Nazmi, Anita L. A. Ruissen, Els Walgreen-Weterings, Jan van Marle, Alexander B. Doust^¶, Wim van't Hof, Jan G. M. Bolscher, and Arie V. Nieuw Amerongen

From the Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam, Vrije Universiteit and Universiteit van Amsterdam, 1081 BT Amsterdam, The Netherlands, the Department of Cell Biology and Histology, Central Electron Microscopy, Academic Medical Center, 1105 AZ Amsterdam, The Netherlands, and the ^¶Department of Physics and Astronomy, Biophysics Section, Vrije Universiteit, 1105 AZ Amsterdam, The Netherlands

Inhibitors of the energy metabolism, such as sodium azide and valinomycin, render yeast cells completely resistant against the killing action of a number of cationic antimicrobial peptides, including the salivary antimicrobial peptide Histatin 5. In this study the Histatin 5-mediated killing of the opportunistic yeast Candida albicans was used as a model system to comprehensively investigate the molecular basis underlying this phenomenon. Using confocal and electron microscopy it was demonstrated that the energy poison azide reversibly blocked the entry of Histatin 5 at the level of the yeast cell wall. Azide treatment hardly induced depolarization of the yeast cell membrane potential, excluding it as a cause of the lowered sensitivity. In contrast, the diminished sensitivity to Histatin 5 of energy-depleted C. albicans was restored by increasing the fluidity of the membrane using the membrane fluidizer benzyl alcohol. Furthermore, rigidification of the membrane by incubation at low temperature or in the presence of the membrane rigidifier Me₂SO increased the resistance against Histatin 5, while not affecting the energy charge of the cell. In line, azide induced alterations in the physical state of the interior of the lipid bilayer. These data demonstrate that changes in the physical state of the membrane underlie the increased resistance to antimicrobial peptides.

Received for publication, November 14, 2006 , and in revised form, April 2, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Member of the Skeletal Tissue Engineering Group Amsterdam. To whom correspondence should be addressed: Academic Centre for Dentistry Amsterdam, Dept. of Oral Biochemistry, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands. Tel.: 31-20-4448672; Fax: 31-20-4448685; E-mail: eci.veerman{at}vumc.nl.

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