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

白色念珠菌细胞表面相关的分泌性天冬氨酸蛋白酶（sap）

• 批准号: 77371039
• 负责人: Professor Dr. Bernhard Hube
• 金额: --
• 依托单位: Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. Hans-Knöll-Institut
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2008
• 资助国家: 德国
• 起止时间: 2007-12-31 至 2011-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/77371039?language=en
• 关键词: Cell; surface; associated; secreted; aspartic

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.

白色念珠菌被认为是健康个体粘膜表面的无害共生菌，但可能引起浅表甚至全身感染。分泌的天冬氨酸蛋白酶（Saps）是促成致病性的属性之一。我们之前的数据表明，Sap9和Sap10是与所有其他Sap9不同的调控性gpi锚定蛋白酶，定位于细胞表面，其靶向真菌来源的蛋白质，涉及细胞表面完整性，细胞分离，粘附和粘膜感染。这些蛋白酶似乎激活、灭活、暴露或掩盖在细胞生物学和宿主真菌相互作用中起关键作用的表面分子。该项目的下一阶段的目标是阐明Sap9和Sap10的底物特异性，鉴定Sap9和Sap10的蛋白靶点，分析这些蛋白靶点的作用，从而阐明Sap9和Sap10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结合来实现，包括生化、硅、蛋白质组学和分子方法。