| Literature DB >> 27044305 |
Yongrong Zhang1, Hanping Feng2.
Abstract
The glucosyltransferase domain ofClostridium difficiletoxins modifies guanine nucleotide-binding proteins of Rho family. It is the major virulent domain of the holotoxins. Various pathogenic effects ofC. difficiletoxins in response to Rho glucosylation have been investigated including cytoskeleton damage, cell death and inflammation. The most recent studies have revealed some significant characteristics of the holotoxins that are independent of glucosylating activity. These findings arouse discussion about the role of glucosyltransferase activity in toxin pathogenesis and open up new insights for toxin mechanism study. In this review, we summarize the pathogenic effects of glucosyltransferase domain of the toxins in the past years. © FEMS 2016. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.Entities:
Keywords: Clostridium difficile; glucosyltransferase; pathogenesis; toxins
Mesh:
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Year: 2016 PMID: 27044305 PMCID: PMC5985493 DOI: 10.1093/femspd/ftw024
Source DB: PubMed Journal: Pathog Dis ISSN: 2049-632X Impact factor: 3.166