Stealth and mimicry by deadly bacterial toxins

Susan P. Yates, René Jørgensen, Gregers R. Andersen, A. Rod Merrill*

*Corresponding author for this work

Research output: Contribution to journalReviewResearchpeer-review

Abstract

Diphtheria toxin and exotoxin A are well-characterized members of the ADP-ribosyltransferase toxin family that function as virulence factors in the pathogenic bacteria Corynebacterium diphtheriae and Pseudomonas aeruginosa. Recent high-resolution structural data of the Michaelis (enzyme-substrate) complex of the P. aeruginosa toxin with an NAD+ analog and eukaryotic elongation factor 2 (eEF2) have provided insights into the mechanism of inactivation of protein synthesis caused by these protein factors. In addition, rigorous steady-state and stopped-flow kinetic analyses of the toxin-catalyzed reaction, in combination with inhibitor studies, have resulted in a quantum leap in our understanding of the mechanistic details of this deadly enzyme mechanism. It is now apparent that these toxins use stealth and molecular mimicry in unleashing their toxic strategy in the infected host eukaryotic cell.

Original languageEnglish
JournalTrends in Biochemical Sciences
Volume31
Issue number2
Pages (from-to)123-133
Number of pages11
ISSN0968-0004
DOIs
Publication statusPublished - Feb 2006
Externally publishedYes

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