Role of MCE domain-containing proteins in Bdellovibrio bacteriovorus

含有MCE结构域的蛋白质，虽然最初被认为在巨噬细胞内结核分枝杆菌的进入和存活中起作用，但后来发现在细菌内的脂质转运中起作用。在大肠杆菌中，已经鉴定出三种含有MCE结构域的蛋白质，它们都参与磷脂在其两层细胞膜之间的运输。然而，这些结构域如何参与运输仍有待阐明。为了进一步了解这一过程，本项目重点研究了掠夺性细菌B. bacteriovorus中含有MCE结构域的蛋白质。卵状芽孢杆菌捕食多种革兰氏阴性菌，在自由生长和捕食之间摇摆不定。生物信息学分析表明，B. Bacteriovorus含有5个MCE结构域，这些MCE结构域的蛋白在生长和捕食阶段表达差异，表明它们在该捕食者的生命周期中具有重要意义。了解其特殊的脂质转运机制以及B. bacteriovorus进入猎物细胞的机制可以为理解MCE结构域蛋白的功能和新一代抗菌药物的开发提供重要的见解。为了分析这些蛋白质的作用，将需要多学科的方法，在生物物理学和分子生物学领域工作，并使用最新的结构生物学技术，包括核磁共振，中子和x射线散射，中子反射计，电子显微镜和x射线晶体学。

MCE domain containing proteins, although initially identified as having a role in the entry and survival of M. tuberculosis inside macrophages, have since been found to have a role in lipid transport within bacteria. In E. coli, three MCE domain containing proteins have been identified, all involved in the transport of phospholipids between its two cell membranes. However how these domains are involved in transport still remains to be elucidated. To provide further insight in to this process, this project focuses on studying the MCE domain containing proteins in the predatory bacterium B. bacteriovorus. B. bacteriovorus preys on a wide range of gram-negative bacteria and oscillates between free-living growth and predation. Bioinformatic analysis has revealed that B. Bacteriovorus contains 5 MCE domain containing proteins that are differentially expressed between growth and predation phases, suggesting their importance in the lifecycle of this predator. Understanding its specialised lipid transport mechanisms and the mechanisms by which B. bacteriovorus enters a prey cell could provide significant insight in to the understanding of how MCE domain containing proteins function and the development of a new generation antimicrobial agents. To analyse the role of these proteins will require a multidisciplinary approach, working in the fields of both biophysics and molecular biology and using the latest structural biology techniques including nuclear magnetic resonance, neutron and X-ray scattering, neutron reflectometry, electron microscopy and X-ray crystallography.