Clostridium perfringens inhibition

Another subfamily of ADP-iibosylating toxins modifies G-actin (at Argl77), thereby inhibiting actin polymerization. Members of this family are, for example, C. botulinum C2 toxin and Clostridium perfringens iota toxin. These toxins are binary in structure. They consist of an enzyme component and a separate binding component, which is structurally related to the binding component of anthrax toxin [3]. 

Smith, L.D.S., Inhibition of Clostridium botulinum by strains of Clostridium perfringens isolated from soil, Appl. Microbiol., 30, 319-323, 1975. 

O Leary, V., and Solberg, M. (1976). Effect of sodium nitrite inhibition on intracellular thiol groups and on the activity of certain glycolytic enzymes in Clostridium perfringens. Appl. Environ. Microbiol. 31, 208-212. 

Geipel U, Just I, Aktories K (1990) Inhibition of cytochalasin D-stimulated G-actin ATPase by ADP-ribosylation with Clostridium perfringens iota toxin. In Biochem. J. 266 335-9... 

X 10 ) and substrate specificities, and exhibited similar behaviour towards ions they differed slightly in pH optima, thermostabilities, and kinetic properties. The neuraminidases differ from Clostridium perfringens neuraminidase (mol. wt. 5.7 X 10 ) in substrate specificity, and were not inhibited by 4-chloro-mercuribenzoate. 

No co-factors were necessary, and the enzymic activity was inhibited by Ca +, Cu +, Fe +, Fe +, and Hg + ions and 4-chloromercuribenzenesulphonic acid. The purified enzyme, like the neuraminidase from Clostridium perfringens, released terminal 5-acetamido-3,5-dideoxy-D- /ycero-D- /ac/o-2-nonulosonic acid residues from the external surface of intact human erythrocytes. 

Muscle aldolase is strongly inhibited by traces of heavy metals and its activity is not decreased by metal binding reagents such as cysteine and a,a -dipyridyl. Yeast aldolase, which has been extensively purified by Warburg, is inactivated by cysteine and reactivated by ferrous, zinc, or cobaltous ion. Aldolase of Clostridium perfringens, on the other hand, is reactivated by ferrous or cobaltous ions in the presence of cysteine. Pea aldolase is not inhibited by heavy metals nor by cysteine and is not activated by ferrous or cobaltous ions. It is puzzling that although each of these aldolases catalyzes the same thermodynamic reaction, they still possess markedly different activation requirements. 

McClane, B. A., 1984, Osmotic stabilizers differentially inhibit permeability alterations induced in Vero cells by Clostridium perfringens enterotoxin, Biochim. Biophys. Acta. 777 99-106. 

Sugimoto, N., Miyamoto, A., Horiguchi, Y, Okabe, T., and Matsuda, M., 1992, Inhibition of neuromuscular transmission in isolated mouse phrenic nerve-diaphragm by the enterotoxin of Clostridium perfringens type A, Toxicon. 30 825-834. 

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