Cell surface associated secreted aspartic proteases (saps) of Candida albicans

白色念珠菌被认为是健康个体粘膜表面的无害寄生物，但可能引起浅表甚至全身感染。分泌型天冬氨酸蛋白酶（SAP）是促成致病性的那些属性之一。我们以前的数据表明，Sap 9和Sap 10，与所有其他的SAP，调节GPI锚定蛋白酶，定位于细胞表面，其目标蛋白的真菌来源的参与细胞表面完整性，细胞分离，粘附和粘膜感染。这些蛋白酶似乎激活，隐藏，暴露或掩盖表面分子，这些分子在细胞生物学和宿主真菌相互作用中起着至关重要的作用。该项目下一阶段的目标是阐明Sap 9和Sap 10的底物特异性，鉴定Sap 9和Sap 10的蛋白质靶点，分析这些蛋白质靶点的作用，从而阐明Sap 9和Sap 10对细胞生物学和宿主-真菌相互作用的贡献。这将通过多种策略的组合来实现，包括生物化学、计算机模拟、蛋白质组学和分子方法。

Candida albicans is considered a harmless commensal of mucosal surfaces of healthy individuals, but may cause superficial or even systemic infections. Secreted aspartic proteases (Saps) are among those attributes which contribute to pathogenicity. Our previous data showed that Sap9 and Sap10 are, in contrast to all other Saps, regulatory GPI-anchored proteases, localised on the cell surface, which target proteins of fungal origin involved in cell surface integrity, cell separation, adhesion and mucosal infection. These proteases seem to activate, inactivate, expose or mask surface molecules which play crucial roles for cell biology and hostfungus interactions. The aim of the next phase of this project is to elucidate the substrate specificities of Sap9 and Sap10, to identify protein targets of Sap9 and Sap10, to analyse the role of these protein targets and thus to elucidate the contributions of Sap9 and Sap10 for cellular biology and host-fungus interactions. This will be achieved using a combination of strategies, including biochemical, in silico, proteomic and molecular approaches.