Differential regulation of SAP8 and SAPS, which encode two new members of the secreted aspartic proteinase family in Candida albicans Monod, Michel and Hube, Bernhard and Hess, Daniela and Sanglard, Dominique,, 144, 2731-2737 (1998), doi = https://doi.org/10.1099/00221287-144-10-2731, publicationName = Microbiology Society, issn = 1350-0872, 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., language=, type=