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Secreted aspartic proteinases (Sap) play a role in the virulence of pathogenic  Candida  spp.  Candida parapsilosis  possesses three genes encoding these enzymes:  SAPP1 ,  SAPP2 , and  SAPP3 . We analyzed the expression of the  SAPP1  and  SAPP2  genes and the production of Sapp1p and Sapp2p proteinases in the presence of different nitrogen sources. While the  SAPP2  transcript was present under all of the conditions tested, expression of  SAPP1  was induced only by the presence of exogenous protein as the sole nitrogen source. The concentration of Sapp1p in the medium upon induction was at least one order of magnitude higher than the concentration of Sapp2p in all media tested in this study. Enzymological characterization of purified Sapp1p and Sapp2p demonstrated that Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than Sapp1p. Homology models of Sapp1p and Sapp2p revealed structural motifs that may be responsible for the differences between these two enzymes. Our results indicate that  C. parapsilosis  secretes a low level of Sapp2p proteinase with narrow substrate specificity and low proteolytic activity under most conditions, while expression and secretion of a higher amount of catalytically efficient Sapp1p enzymes is triggered in the presence of exogenous protein serving as a nitrogen source.

Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties