Bacterial toxin and effector glycosyltransferases

被引：37

作者：

Belyi, Yury ^{[2
]}

Aktories, Klaus ^{[1
]}

机构：

[1] Univ Freiburg, Inst Expt & Klin Pharmakol & Toxikol, D-79104 Freiburg, Germany

[2] Gamaleya Res Inst, Moscow 123098, Russia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2010年 / 1800卷 / 02期

关键词：

Glycosyltransferase; Rho protein; Bacterial protein toxin; Glucosylation; Clostridial glucosylating toxin; Clostridium difficile toxin; Legionella pneumophila; Elongation factor 1A; CLOSTRIDIUM-DIFFICILE TOXIN; SORDELLII LETHAL TOXIN; ELONGATION-FACTOR; 1A; LEGIONELLA-PNEUMOPHILA; RHO-GTPASES; CONFORMATIONAL-CHANGES; LEGIONNAIRES-DISEASE; NUCLEOTIDE EXCHANGE; BINDING-SITE; TRANSFER-RNA;

D O I：

10.1016/j.bbagen.2009.07.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Clostridial glucosylating cytotoxins, including Clostridium difficile toxins A and B, Clostridium novyi a-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. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：134 / 143

页数：10

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