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Analysis of export and membrane association of PlaB - a surface-associated phospholipase A and virulence factor of Legionella pneumophila

PlaB（一种表面相关磷脂酶 A 和嗜肺军团菌毒力因子）的输出和膜关联分析

基本信息

批准号：
16256777
负责人：
Professorin Dr. Antje Flieger
金额：
--
依托单位：
Fachgebiet 11: Bakterielle darmpathogene Erreger und Legionellen
依托单位国家：
德国
项目类别：
Research Grants
财政年份：
2005
资助国家：
德国
起止时间：
2004-12-31 至 2018-12-31
项目状态：
已结题

来源：
https://gepris.dfg.de/gepris/projekt/16256777?language=en
关键词：
Analysis export membrane association PlaB

项目摘要

Legionellae are intracellular pathogens and the causative agent of Legionnaires disease, a potentially fatal pneumonia. At least 18 different phospholipases including PlaB, a hemolytic phospholipase A, have been described for Legionella pneumophila. Recent analysis showed that PlaB-derived activity promotes virulence and is activated by a novel oligomer dissociation mechanism. Further, PlaB localizes to the bacterial surface although no signal peptide is predicted, the N-terminal region remains uncleaved, and the first 20 amino acids are not essential for export to the surface. Additionally, PlaB associates with membranes although no transmembrane domains, beta-barrel structures, typical signatures or modifications of lipoproteins have been found. This indicates that PlaB is not an integral but rather a peripheric membrane-associated protein and so far unknown interactions with membrane proteins or lipids accomplish membrane association. Since, none of the currently known secretion modes in L. pneumophila drives PlaB export to the surface, I hypothesize that a novel export mechanism is responsible for PlaB surface presentation. In the here presented project: 1) the L. pneumophila determinants and the regions within PlaB driving PlaB export to the surface, 2) interactors responsible for PlaB association with the membrane and respective PlaB regions involved, and 3) the contribution of the oligomeric state to export and membrane association will be analyzed.

军团菌是细胞内病原体，是军团菌病（一种潜在致命性肺炎）的病原体。至少有18种不同的磷脂酶，包括PlaB，溶血性磷脂酶A，已被描述为嗜肺军团菌。最近的分析表明，PlaB衍生的活性促进毒力，并通过一种新的寡聚体解离机制激活。此外，PlaB定位于细菌表面，尽管没有预测到信号肽，N-末端区域保持未切割，并且前20个氨基酸对于输出到表面不是必需的。此外，尽管没有发现跨膜结构域、β-桶结构、脂蛋白的典型特征或修饰，但PlaB与膜结合，这表明PlaB不是一个完整的膜结合蛋白，而是一个外周膜结合蛋白，迄今为止，PlaB与膜蛋白或脂质的相互作用还不清楚。目前已知的L. pneumophila驱动PlaB出口到表面，我假设一种新的出口机制是负责PlaB表面介绍。在本项目中：1）L。将分析嗜肺菌决定子和PlaB内驱动PlaB输出到表面的区域，2）负责PlaB与膜和所涉及的相应PlaB区域缔合的相互作用物，和3）寡聚状态对输出和膜缔合的贡献。