Bidirectional attack on the actin cytoskeleton. Bacterial protein toxins causing polymerization or depolymerization of actin

Toxicon. 2012 Sep 15;60(4):572-81. doi: 10.1016/j.toxicon.2012.04.338. Epub 2012 Apr 19.

Abstract

The actin cytoskeleton is one of the major targets of bacterial protein toxins. The family of binary actin-ADP-ribosylating toxins, including Clostridium difficile transferase CDT, Clostridium perfringens iota toxin and Clostridium botulinum C2 toxin, modifies arginine-177 of actin. Thereby actin polymerization is blocked. By contrast, actin polymerization is facilitated by the tripartite Photorhabdus luminescens toxin complex including TccC3, which modifies actin at threonine-148. The review discusses both toxin families in respect to recent findings.

Publication types

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

MeSH terms

  • ADP Ribose Transferases / chemistry
  • ADP Ribose Transferases / metabolism
  • Actin Cytoskeleton / chemistry*
  • Arginine / chemistry
  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / metabolism
  • Botulinum Toxins / chemistry
  • Botulinum Toxins / metabolism
  • Clostridioides difficile / metabolism*
  • Photorhabdus / metabolism*
  • Polymerization
  • Protein Conformation
  • Transferases / chemistry
  • Transferases / metabolism

Substances

  • Bacterial Toxins
  • iota toxin, Clostridium perfringens
  • Arginine
  • Transferases
  • ADP Ribose Transferases
  • Botulinum Toxins
  • botulinum toxin type C