Institut Curie, Centre de Recherche, Paris, France.
Mol Microbiol. 2010 Mar;75(6):1327-36. doi: 10.1111/j.1365-2958.2010.07064.x. Epub 2010 Feb 4.
Although much is known about the structure and biosynthesis of microbial cell envelope constituents, the three-dimensional organization, assembly and interactions of the individual components remain poorly understood. How do cell walls remodel during cell growth or incubation with drugs? What is the supramolecular architecture of proteins in bacterial surface layers, in outer membranes and in intracytoplasmic membranes? What is the spatial arrangement of cell surface receptors, clustered or homogeneous? What are the adhesive and mechanical properties of cell surface proteins and how are they related to function? Traditionally, these questions have been difficult - or impossible - to address owing to the lack of high-resolution single-cell and single-molecule probing techniques. With its ability to observe and force probe the cell envelope down to the molecular level under physiological conditions, atomic force microscopy (AFM) has recently offered new opportunities in molecular microbiology. While high-resolution AFM imaging is a powerful tool for visualizing the architecture of cells and membranes in buffer solution, force spectroscopy offers a means to analyse the localization, interactions and elasticity of their individual constituents. These nanoscale experiments complement microscopy, genetics and biochemical methods traditionally used to analyse the microbial envelope.
虽然人们对微生物细胞包膜成分的结构和生物合成了解很多，但单个成分的三维组织、组装和相互作用仍知之甚少。细胞壁在细胞生长或与药物孵育期间如何重塑？细菌表面层、外膜和细胞内膜中的蛋白质的超分子结构是什么？细胞表面受体是聚集的还是均匀分布的？细胞表面蛋白的粘附和力学性质如何，它们与功能有何关系？传统上，由于缺乏高分辨率单细胞和单分子探测技术，这些问题很难（或不可能）解决。原子力显微镜（AFM）具有在生理条件下观察和强制探测细胞包膜至分子水平的能力，最近为分子微生物学提供了新的机会。虽然高分辨率 AFM 成像技术是可视化缓冲溶液中细胞和膜结构的有力工具，但力谱分析提供了一种分析其单个成分的定位、相互作用和弹性的方法。这些纳米级实验补充了传统上用于分析微生物包膜的显微镜、遗传学和生化方法。
