Secreted aspartyl proteinase 2 (Sap2)

Secreted aspartyl proteinase 2 is the major secreted aspartyl protease produced by Candida albicans in vitro and in many infection contexts[1][2]. It exhibits broad substrate specificity, capable of degrading numerous human proteins, including immunoglobulins, mucins, extracellular matrix components (such as keratin, collagen, and vimentin), and host defense molecules (like lactoferrin and complement)[2]. By breaking down these proteins, Sap2 enables nutrient acquisition, deep tissue penetration, and evasion of host immune responses, playing a critical role in Candida pathogenicity[1][2]. Expression is tightly regulated by nutrient availability and signaling pathways, such as TOR and amino acid-sensing mechanisms[1]. Loss of SAP2 dramatically reduces virulence in animal models[1], underscoring its significance as a therapeutic target. Structural studies have revealed unique features distinguishing Sap2 from other aspartyl proteases, contributing to its broad substrate profile[2].

Other names

Sap2SAP2 (when referring to the gene)secreted aspartic protease 2

Enzyme inhibition (drugs act by inhibiting the proteolytic activity of Sap2, blocking protein degradation essential for fungal virulence and growth)[2]