The predicted secretome of the opportunistic fungal pathogen Candida albicans contains more than 200 ORFs of diverse and often unknown function. Majority of the secreted proteins that have been experimentally evaluated to date are hydrolytic enzymes (proteinases, phospholipases and lipases). Acting on the interface between the pathogen and the host, the secreted hydrolases may enable invasion of host tissues, help the pathogen to avoid host defense mechanisms, or allow the microorganism to utilize host cell macromolecules as a source of nutrients. Aspartic proteinases constitute the best-characterized family of the C. albicans secreted proteins. Number of studies addressed also secreted phospholipases. Lipases and N-acetylhexosaminidase have received less attention thus far. Many ORFs that are predicted to encode secreted proteins await characterization.

Gilead Sciences Research Center Institute of Organic Chemistry and Biochemistry Academy of Sciences of the Czech Republic Flemingovo namesti 2 166 10 Prague 6 Czech Republic

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Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p from Candida parapsilosis

Characterization of the Candida albicans Amino Acid Permease Family: Gap2 Is the Only General Amino Acid Permease and Gap4 Is an S-Adenosylmethionine (SAM) Transporter Required for SAM-Induced Morphogenesis

Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition

Evidence for the presence of proteolytically active secreted aspartic proteinase 1 of Candida parapsilosis in the cell wall

The Candida albicans GAP gene family encodes permeases involved in general and specific amino acid uptake and sensing