Belyi Yury, Aktories Klaus
Gamaleya Research Institute, Moscow 123098, Russia.
Biochim Biophys Acta. 2010 Feb;1800(2):134-43. doi: 10.1016/j.bbagen.2009.07.022. Epub 2009 Jul 30.
Clostridial glucosylating cytotoxins, including Clostridium difficile toxins A and B, Clostridium novyi alpha-toxin, and Clostridium sordellii lethal toxin, are major virulence factors and causative agents of human diseases. These toxins mono-O-glucosylate (or mono-O-GlcNAcylate) a specific threonine residue of Rho/Ras-proteins, which is essential for the function of the molecular switches. Recently, a related group of glucosyltransferases from Legionella pneumophila has been identified. These Legionella glucosyltransferases modify the large GTPase elongation factor eEF1A at a serine residue by mono-O-glucosylation, thereby inhibiting protein synthesis of target cells. Recent results on structures, functions and biological roles of both groups of bacterial toxin glucosyltransferases will be discussed.
梭菌属糖基化细胞毒素,包括艰难梭菌毒素A和B、诺维氏梭菌α毒素以及索氏梭菌致死毒素,是人类疾病的主要毒力因子和病原体。这些毒素对Rho/Ras蛋白的特定苏氨酸残基进行单O-糖基化(或单O-GlcNAc化),这对分子开关的功能至关重要。最近,已鉴定出一组来自嗜肺军团菌的相关糖基转移酶。这些军团菌糖基转移酶通过单O-糖基化修饰大GTPase延伸因子eEF1A的丝氨酸残基,从而抑制靶细胞的蛋白质合成。将讨论这两组细菌毒素糖基转移酶的结构、功能和生物学作用的最新研究结果。