Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity

Robert Considine, Lance L. Simpson

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

Review article-Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity. Toxicon 29, 913-936, 1991.-Clostridial organisms produce a number of binary toxins. Thus far, three complete toxins (botulinum, perfringens and spiroforme) and one incomplete toxin (difficile) have been identified. In the case of complete toxins, there is a heavy chain component (Mr ∼ 100,000) that binds to target cells and helps create a docking site for the light chain component (Mr ∼ 50,000). The latter is an enzyme that possesses mono(ADP-ribosyl)transferase activity. The toxins appear to proceed through a three step sequence to exert their effects, including a binding step, an internalization step and an intracellular poisoning step. The substrate for the toxins is G-actin. By virtue of ADP-ribosylating monomeric actin, the toxins prevent polymerization as well as promoting depolymerization. The most characteristic cellular effect of the toxins is alteration of the cytoskeleton, which leads directly to changes in cellular morphology and indirectly to changes in cell function (e.g. release of chemical mediators). Binary toxins capable of modifying actin are likely to be useful tools in the study of cell biology.

Original languageEnglish (US)
Pages (from-to)913-936
Number of pages24
JournalToxicon
Volume29
Issue number8
DOIs
StatePublished - 1991
Externally publishedYes

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ADP Ribose Transferases
Actins
Cytology
Depolymerization
Botulinum Toxins
Cytoskeleton
Polymerization
Adenosine Diphosphate
Poisoning
Cell Biology
Light
Substrates
Enzymes

ASJC Scopus subject areas

  • Toxicology

Cite this

Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity. / Considine, Robert; Simpson, Lance L.

In: Toxicon, Vol. 29, No. 8, 1991, p. 913-936.

Research output: Contribution to journalArticle

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