Bacterial Toxins Modifying the Actin Cytoskeleton

Int Microbiol. 1999 Sep;2(3):185-94.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP Ribose Transferases*
  • Actin Cytoskeleton / drug effects*
  • Actins / metabolism
  • Animals
  • Bacillus / metabolism
  • Bacillus / pathogenicity
  • Bacterial Toxins / pharmacology*
  • Binding Sites
  • Biopolymers
  • Botulinum Toxins / pharmacology
  • Cadherins / metabolism
  • Cell Line
  • Clostridium / metabolism
  • Clostridium / pathogenicity*
  • Cytotoxins / pharmacology
  • Dogs
  • Escherichia coli / metabolism
  • Escherichia coli / pathogenicity
  • Escherichia coli Proteins*
  • Glycosylation
  • Humans
  • Poly(ADP-ribose) Polymerases / physiology
  • rho GTP-Binding Proteins / antagonists & inhibitors

Substances

  • Actins
  • Bacterial Toxins
  • Biopolymers
  • Cadherins
  • Cytotoxins
  • Escherichia coli Proteins
  • cytotoxic necrotizing factor type 2
  • iota toxin, Clostridium perfringens
  • cytotoxic necrotizing factor type 1
  • ADP Ribose Transferases
  • Poly(ADP-ribose) Polymerases
  • Botulinum Toxins
  • rho GTP-Binding Proteins
  • botulinum toxin type C