作者: D. Alsteens , M. C. Garcia , P. N. Lipke , Y. F. Dufrene
关键词:
摘要: Understanding how cell adhesion proteins form domains is a key challenge in biology. Here, we use single-molecule atomic force microscopy (AFM) to demonstrate the force-induced formation and propagation of nanodomains living fungal cells, focusing on covalently anchored cell-wall protein Als5p from Candida albicans. We show that pulling single adhesins with AFM tips terminated specific antibodies triggers 100-500 nm propagate over entire surface. Control experiments (with cells lacking Als5p, single-site mutation protein, bare tips, modified irrelevant antibodies) result redistribution triggered by conformational changes initially probed proteins, rather than nonspecific perturbations. remodeling independent cellular metabolic activity because heat-killed same behavior as live cells. Using fluorescence microscopy, also find are formed within ∼30 min migrate at speed ∼20 nm·min(-1), indicating domain slow, time-dependent processes. These results mechanical stimuli can trigger suggest clustering may be mechanism for activating adhesion.