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Stealth and mimicry by deadly bacterial toxins

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskning

  • S.P. Yates, Uni. Guelph, Canada
  • Rene Jørgensen, Danmark
  • Gregers Rom Andersen
  • A.R. Merrill, Uni. Guelph, Canada
  • Det Naturvidenskabelige Fakultet
  • Molekylærbiologisk Institut
Diphtheria toxin and exotoxin A are well-characterized members of the ADP-ribosyltransferase toxin family that serve as virulence factors in the pathogenic bacteria, Corynebacterium diphtheriae and Pseudomonas aeruginosa.  New high-resolution structural data of the Michaelis complex of the Pseudomonas toxin with an NAD+ analogue and eukaryotic elongation factor 2 have provided new insights into the mechanism of inactivation of protein synthesis caused by these protein factors.  Concomitantly, rigorous steady-state and stopped flow kinetic analyses of the toxin-catalyzed reaction, in combination with inhibitor studies, has resulted in a quantum leap in our understanding of the mechanistic details of this deadly enzyme mechanism.  Furthermore, it is now apparent that these toxins use stealth and molecular mimicry in unleashing their toxic strategy within the infected host eukaryotic cell.
OriginalsprogEngelsk
TidsskriftTrends in Biochemical Sciences
Vol/bind31
Sider (fra-til)123-133
Antal sider11
StatusUdgivet - 2006

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