| Literature DB >> 19647041 |
Abstract
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. Copyright 2009 Elsevier B.V. All rights reserved.Entities:
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Year: 2009 PMID: 19647041 DOI: 10.1016/j.bbagen.2009.07.022
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002