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1Service de Dermatologie (DHURDV), Laboratoire de Mycologiel, and lnstitut de Microbiologie
2lnstitut fur Allgemeine Botanik, Angewandte Molekularbiologie 111, Universitdt Hamburg, Hamburg, Germany
3Centre Hospitalier Universitaire Vaudois, 101 1 Lausanne, Switzerland
1 Author for correspondence: Michel Monod. Tel: +4121 314 0376. Fax: +41 21 314 0378. e-mail: Michel.Monod@chuv.hospvd.ch
ABSTRACT
SUMMARY: Secreted aspartic proteinases (Saps) contribute to the virulence of Candida albicans in systemic animal models of infection. Seven genes encoding Saps (SAM-SAP7) have been identified to date but evidence suggested the existence of additional SAP genes. The screening of a C. albicans iZEMBL3 genomic library for the presence of other SAP genes was undertaken. Two new genes, SAP8 and SAPS, were isolated. The N-terminal amino acid sequence deduced from SAP8 downstream of a Kex2plike cleavage site corresponds to the N-terminal amino acid sequence of the 41 kDa Sap isolated and characterized previously. SAP8 mRNA was expressed preferentially in yeasts at 25 "C after 6 and 9 h growth in BSA-containing medium. SAPS encodes an aspartic proteinase with a Kex2pllike cleavage site and contains a putative glycophosphatidylinositol-anchor signal at the C-terminus. Although the SAPS gene product has not yet been isolated from cultures of C. albicans, transcripts of SAPS were observed preferentially in later growth phases when SAP8 expression had decreased.
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