Differential Requirement for the Translocation of Clostridial Binary Toxins: Iota Toxin Requires a Membrane Potential Gradient

Abstract

Clostridial binary toxins, such as Clostridium perfringens Iota and Clostridium botulinum C2, are composed of a binding protein (Ib and C2-II, respectively) that recognizes distinct membrane receptors and mediates internalization of a catalytic protein (Ia and C2-I, respectively) with ADP-ribosyltransferase activity that depolymerizes the actin cytoskeleton. After internalization, it was found that C2 and Iota toxins were not routed to the Golgi apparatus and exhibited differential sensitivity to inhibitors of endosome acidification. While the C2-I component of C2 toxin was translocated into the cytosol from early endosomes, translocation of the Ia component of Iota toxin occurred between early and late endosomes, was dependent on more acidic conditions, and uniquely required a membrane potential gradient.

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Document Details

Document Type
Technical Report
Publication Date
Feb 28, 2007
Accession Number
ADA464810

Entities

People

  • Bradley G. Stiles
  • Christophe Lamaze
  • Jean Marvaud
  • Martha L Hale
  • Maryse Gibert
  • Michel R. Popoff
  • Patrice Boquet
  • Yannick Pereira

Organizations

  • United States Army Medical Research Institute of Infectious Diseases

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Bacterial Toxins
  • Cell Membrane
  • Cells
  • Cellular Structures
  • Chemistry
  • Clostridium
  • Cytoskeleton
  • Endosomes
  • Golgi Apparatus
  • Inhibitors
  • Membrane Potentials
  • Membranes
  • Molecules
  • Organelles
  • Proteins

Fields of Study

  • Biology
  • Computer science

Readers

  • Analytical Mechanics
  • Microbial Pathology
  • Molecular and Cellular Biochemistry