Bacterial toxins modifying the actin cytoskeleton

Authors

  • Jean-François Richard Institut des Neurosciences, Université Pierre et Marie Curie, CNRS UMR7624, Paris, France
  • Laetitia Petit Unité des Toxines Microbiennes, Institut Pasteur, Paris, France
  • Maryse Gibert Unité des Toxines Microbiennes, Institut Pasteur, Paris, France
  • Jean Christophe Marvaud Unité des Toxines Microbiennes, Institut Pasteur, Paris, France
  • Claude Bouchaud Unité des Toxines Microbiennes, Institut Pasteur, Paris, France
  • Michel R. Popoff Unité des Toxines Microbiennes, Institut Pasteur, Paris, France

Keywords:

toxins, actin, rho proteins, ras proteins, intercellular junction

Abstract

Numerous bacterial toxins recognize the actin cytoskeleton as a target. The clostridial binary toxins (Iota and C2 families) ADP-ribosylate the actin monomers causing the dissociation of the actin filaments. The large clostridial toxins from Clostridium difficile, Clostridium sordellii and Clostridium novyi inactivate, by glucosylation, proteins from the Rho family that regulate actin polymerization. In contrast, the cytotoxic necrotic factor from Escherichia coli activates Rho by deamidation and increases the formation of actin filaments. The enterotoxin of Bacteroides fragilis is a protease specific for E-cadherin and it promotes the reorganization of the actin cytoskeleton. The bacterial toxins that modify the actin cytoskeleton induce various cell disfunctions including changes in cell barrier permeability and disruption of intercellular junctions.

Downloads

Published

2010-03-16

Issue

Section

Review Articles