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Background  The polymorphic species  Candida albicans  is the major cause of candidiasis in humans. The secreted aspartyl proteinases (Saps) of  C. albicans , encoded by a family of 10  SAP  genes, have been investigated as the virulent factors during candidiasis. However, the biological functions of most Sap proteins are still uncertain. In this study, we applied co-culture system of  C. albicans  and THP-1 human monocytes to explore the pathogenic roles and biological functions of Sap proteinases.    Results  After 1 hr of co-culture of  C. albicans  strains and THP-1 human monocytes at 37°C, more than 60% of the THP-1-engulfed wild type and Δ sap5 Candida  cells were developing long hyphae. However, about 50% of THP-1-engulfed Δ sap6 Candida  cells were generating short hyphae, and more dead  Candida  cells were found in Δ sap6  strain that was ingested by THP-1 cells (about 15% in Δ sap6  strain vs. 2 ~ 2.5% in  SC5314  and Δ sap5  strains). The immunofluorescence staining demonstrated that the Sap6 is the major hyphal tip located Sap protein under THP-1 phagocytosis. The  sap6 -deleted strains (Δ sap6 , Δ sap4/6 , and Δ sap5/6 ) appeared slower growth on Congo red containing solid medium at 25°C, and the growth defect was exacerbated when cultured at 37°C in Congo red or SDS containing medium. In addition, more proteins were secreted from Δ sap6  strain and the β-mercaptoethanol (β-ME) extractable surface proteins from Δ sap6  mutant were more abundant than that of extracted from wild type strain, which included the plasma membrane protein (Pma1p), the ER-chaperone protein (Kar2p), the protein transport-related protein (Arf1p), the cytoskeleton protein (Act1), and the mitochondrial outer membrane protein (porin 1). Moreover, the cell surface accessibility was increased in  sap6 -deleted strains.    Conclusion  From these results, we speculated that the cell surface constitution of  C. albicans  Δ sap6  strain was defect. This may cause the more accessible of β-ME to disulfide-bridged cell surface components and may weaken the resistance of Δ sap6  strain encountering phagocytosis of THP-1 cells. Sap6 protein displays a significant function involving in maintenance the cell surface integrity.

Sap6, a secreted aspartyl proteinase, participates in maintenance the cell surface integrity of Candida albicans