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Aggregation of yeast cells: direct measurement of discrete lectin-carbohydrate interactions.

机译:酵母细胞的聚集:直接测量离散的凝集素与碳水化合物的相互作用。

摘要

Aggregation of microbial cells mediated by specific interactions plays a pivotal role in the natural environment, in medicine and in biotechnological processes. Here we used atomic force microscopy (AFM) to measure individual lectin-carbohydrate interactions involved in the flocculation of yeast cells, an aggregation event of crucial importance in fermentation technology. AFM probes functionalized with oligoglucose carbohydrates were used to record force-distance curves on living yeast cells at a rate of 0.5 micro m s(-1). Flocculating cells showed adhesion forces of 121+/-53 pN, reflecting the specific interaction between individual cell-surface lectins and glucose residues. Similar adhesion forces, 117+/-41 pN, were measured using probes functionalized with the lectin concanavalin A and attributed to specific binding to cell-surface mannose residues. By contrast, specific interaction forces were not observed in non-flocculating conditions, i.e. in the presence of mannose or when using non-flocculating cells, pointing to their involvement in yeast flocculation. The single molecule force spectroscopy measurements presented here provide a means to study a variety of cellular interactions at the molecular level, such as the adhesion of bacteria to animal and plant tissues.
机译:由特定相互作用介导的微生物细胞的聚集在自然环境,医学和生物技术过程中起着关键作用。在这里,我们使用原子力显微镜(AFM)来测量参与酵母细胞絮凝的凝集素与碳水化合物的相互作用,这是发酵技术中至关重要的聚集事件。用寡糖碳水化合物功能化的AFM探针用于以0.5 micro m s(-1)的速率记录活酵母细胞上的力-距离曲线。絮凝细胞显示出121 +/- 53 pN的粘附力,反映了单个细胞表面凝集素和葡萄糖残基之间的特异性相互作用。使用被凝集素伴刀豆球蛋白A功能化并且归因于与细胞表面甘露糖残基的特异性结合的探针测量了相似的粘附力117 +/- 41 pN。相反,在非絮凝条件下,即在甘露糖存在下或使用非絮凝细胞时,未观察到特定的相互作用力,表明它们参与了酵母絮凝。本文介绍的单分子力谱测量提供了一种在分子水平上研究各种细胞相互作用的方法,例如细菌对动植物组织的粘附。

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