Merino Susana, Tomás Juan M
Department of Microbiology, Faculty of Biology, University of Barcelona, Diagonal 643, Barcelona 08071, Spain.
Int J Mol Sci. 2014 Feb 19;15(2):2840-57. doi: 10.3390/ijms15022840.
Protein glycosylation had been considered as an eccentricity of a few bacteria. However, through advances in analytical methods and genome sequencing, it is now established that bacteria possess both N-linked and O-linked glycosylation pathways. Both glycosylation pathways can modify multiple proteins, flagellins from Archaea and Eubacteria being one of these. Flagella O-glycosylation has been demonstrated in many polar flagellins from Gram-negative bacteria and in only the Gram-positive genera Clostridium and Listeria. Furthermore, O-glycosylation has also been demonstrated in a limited number of lateral flagellins. In this work, we revised the current advances in flagellar glycosylation from Gram-negative bacteria, focusing on the structural diversity of glycans, the O-linked pathway and the biological function of flagella glycosylation.
蛋白质糖基化曾被认为是少数细菌的一种特殊现象。然而,随着分析方法和基因组测序技术的进步,现在已经确定细菌拥有N-连接和O-连接糖基化途径。这两种糖基化途径都可以修饰多种蛋白质,古细菌和真细菌的鞭毛蛋白就是其中之一。鞭毛O-糖基化已在许多革兰氏阴性菌的极鞭毛蛋白中得到证实,并且仅在革兰氏阳性菌的梭菌属和李斯特菌属中得到证实。此外,在少数侧鞭毛蛋白中也证实了O-糖基化。在这项工作中,我们回顾了革兰氏阴性菌鞭毛糖基化的当前进展,重点关注聚糖的结构多样性、O-连接途径以及鞭毛糖基化的生物学功能。