A family of killer toxins: Exploring the mechanism of ADP-ribosylating toxins

Kenneth P. Holbourn, Clifford Shone, K. R. Acharya*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

107 Citations (Scopus)

Abstract

The ADP-ribosylating toxins (ADPRTs) are a family of toxins that catalyse the hydrolysis of NAD and the transfer of the ADP-ribose moiety onto a target. This family includes many notorious killers, responsible for thousands of deaths annually including: cholera, enterotoxic Escherichia coli, whooping cough, diphtheria and a plethora of Clostridial binary toxins. Despite their notoriety as pathogens, the ADPRTs have been extensively used as cellular tools to study and elucidate the functions of the small GTPases that they target. There are four classes of ADPRTs and at least one structure representative of each of these classes has been determined. They all share a common fold and several motifs around the active site that collectively facilitate the binding and transfer of the ADP-ribose moiety of NAD to their protein targets. In this review, we present an overview of the physiology and cellular qualities of the bacterial ADPRTs and take an in-depth look at the structural motifs that differentiate the different classes of bacterial ADPRTs in relation to their function.

Original languageEnglish
Pages (from-to)4579-4593
Number of pages15
JournalFEBS Journal
Volume273
Issue number20
DOIs
Publication statusPublished - Oct 2006

Keywords

  • ADP-ribosylating toxin
  • ADP-ribosyltransferase
  • GTPases
  • NAD binding
  • Structure

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