Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity. 1991

R V Considine, and L L Simpson
Department of Physiology, Jefferson Medical College, Philadelphia, PA.

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 approximately 100,000) that binds to target cells and helps create a docking site for the light chain component (Mr approximately 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.

UI MeSH Term Description Entries
D011065 Poly(ADP-ribose) Polymerases Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE. ADP-Ribosyltransferase (Polymerizing),Poly ADP Ribose Polymerase,Poly(ADP-Ribose) Synthase,Poly(ADP-ribose) Polymerase,PARP Polymerase,Poly ADP Ribose Transferase,Poly ADP-Ribose Synthase,Poly(ADP-Ribose) Transferase,Poly(ADPR) Polymerase,Poly(ADPribose) Polymerase,Poly ADP Ribose Synthase,Polymerase, PARP,Synthase, Poly ADP-Ribose
D003013 Clostridium A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001427 Bacterial Toxins Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases. Bacterial Toxin,Toxins, Bacterial,Toxin, Bacterial
D036002 ADP Ribose Transferases Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains. ADP-Ribosyltransferase,Mono(ADP-Ribose) Transferases,NAD(P)(+)-Arginine ADP-Ribosyltransferase,NAD+ ADP-Ribosyltransferase,ADP Ribose Transferase,ADPRT,ADPRTs,ART Transferase,ART Transferases,ARTase,ARTases,Mono ADP-ribose Transferases,Mono ADPribose Transferase,Mono ADPribose Transferases,Mono(ADP-Ribose) Transferase,Mono(ADP-Ribosyl)transferase,Mono(ADPribosyl)transferase,Mono-ADP-Ribosyltransferase,MonoADPribosyltransferase,NAD ADP-Ribosyltransferase,NAD(+)-L-arginine ADP-D-ribosyltransferase,NAD-Agmatine ADP-Ribosyltransferase,NAD-Arginine ADP-Ribosyltransferase,NADP-ADPRTase,NADP-Arginine ADP-Ribosyltransferase,ADP Ribosyltransferase,ADP-Ribosyltransferase, NAD,ADP-Ribosyltransferase, NAD+,ADP-Ribosyltransferase, NAD-Agmatine,ADP-Ribosyltransferase, NAD-Arginine,ADP-Ribosyltransferase, NADP-Arginine,ADP-ribose Transferases, Mono,ADPribose Transferase, Mono,ADPribose Transferases, Mono,Mono ADP Ribosyltransferase,Mono ADP ribose Transferases,NAD ADP Ribosyltransferase,NAD Agmatine ADP Ribosyltransferase,NAD Arginine ADP Ribosyltransferase,NAD+ ADP Ribosyltransferase,NADP ADPRTase,NADP Arginine ADP Ribosyltransferase,Ribose Transferase, ADP,Ribose Transferases, ADP,Transferase, ADP Ribose,Transferase, ART,Transferase, Mono ADPribose,Transferases, ADP Ribose,Transferases, ART,Transferases, Mono ADP-ribose,Transferases, Mono ADPribose

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