Pathogenic effects of glucosyltransferase from Clostridium difficile toxins

Pathog Dis. 2016 Jun;74(4):ftw024. doi: 10.1093/femspd/ftw024. Epub 2016 Apr 4.

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.

Keywords: Clostridium difficile; glucosyltransferase; pathogenesis; toxins.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Bacterial Toxins / metabolism*
  • Cell Death
  • Clostridioides difficile / physiology*
  • Cytokines / metabolism
  • Cytoskeleton
  • Disease Models, Animal
  • Enterocolitis, Pseudomembranous / metabolism
  • Enterocolitis, Pseudomembranous / microbiology*
  • Enterocolitis, Pseudomembranous / pathology
  • Glucosyltransferases / metabolism*
  • Humans
  • Inflammation Mediators / metabolism

Substances

  • Bacterial Toxins
  • Cytokines
  • Inflammation Mediators
  • Glucosyltransferases