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J. Biol. Chem., Vol. 281, Issue 2, 688-694, January 13, 2006
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Glycosylphosphatidylinositol-anchored Proteases of Candida albicans Target Proteins Necessary for Both Cellular Processes and Host-Pathogen Interactions*
1
From the
Robert Koch-Institut, D-13353 Berlin, Germany, Molecular Phytopathology and Genetics, University of Hamburg, D-22609 Hamburg, Germany, ¶Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic, ||Department of Oral Medicine and Pathology, Kings College London, SE1 9RT London, United Kingdom, **Department of Dermatology, University of Tuebingen, D-72076 Tuebingen, Germany, University of Amsterdam, 1018 WV Amsterdam, The Netherlands, Aberdeen Fungal Group, School of Medical Sciences, University of Aberdeen, AB25 2ZD Aberdeen, Scotland, United Kingdom, and ¶¶Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland
Intracellular and secreted proteases fulfill multiple functions in microorganisms. In pathogenic microorganisms extracellular proteases may be adapted to interactions with host cells. Here we describe two cell surface-associated aspartic proteases, Sap9 and Sap10, which have structural similarities to yapsins of Saccharomyces cerevisiae and are produced by the human pathogenic yeast Candida albicans. Sap9 and Sap10 are glycosylphosphatidylinositol-anchored and located in the cell membrane or the cell wall. Both proteases are glycosylated, cleave at dibasic or basic processing sites similar to yapsins and Kex2-like proteases, and have functions in cell surface integrity and cell separation during budding. Overexpression of SAP9 in mutants lacking KEX2 or SAP10, or of SAP10 in mutants lacking KEX2 or SAP9, only partially restored these phenotypes, suggesting distinct target proteins of fungal origin for each of the three proteases. In addition, deletion of SAP9 and SAP10 modified the adhesion properties of C. albicans to epithelial cells and caused attenuated epithelial cell damage during experimental oral infection suggesting a unique role for these proteases in both cellular processes and host-pathogen interactions.
Received for publication, August 23, 2005 , and in revised form, October 27, 2005.
* This work was supported by Grants Hu528/8 and Scha 897/1 from the Deutsche Forschungsgemeinschaft (to B. H. and M. S.), 303/04/0432 from the Grant Agency of the Czech Republic (to I. P.), and QLK2-2000-00795 and MRTN-CT-2003-504148 ("Galar Fungail consortium") from the European Commission. 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 To whom correspondence should be addressed: Robert-Koch-Institut, FG16, Nordufer 20, D-13353 Berlin, Germany. Tel.: 49-18887542116; Fax: 49-18887542605; E-mail: HubeB{at}rki.de.
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