This study identified a functional spo0A ORF in enterotoxigenic Clostridium perfringens type A. To evaluate the function of spo0A, an isogenic spo0A knock-out mutant was constructed. The spo0A mutant was unable to form endospores and produce enterotoxin, however, these defects could be restored by complementing the mutant with a recombinant plasmid carrying the wild-type spo0A gene. These resul...

Lucena R.B., Farias L., Libardoni F., Vargas A.C. Giaretta P.R. & Barros C.S.L. 2011. Necrotizing enteritis associated with Clostridium perfringens Type B in chinchillas (Chinchilla lanigera). Pesquisa Veterinária Brasileira 31(12):1071-1074. Departamento de Patologia, Universidade Federal de Santa Maria, Camobi, Santa Maria, RS 97105900, Brazil. E-mail: [email protected] Four 3-4 mont...

The epidemiological and bacteriological investigations on four foodborne outbreaks caused by a new type of enterotoxin-producing Clostridium perfringens are described. C. perfringens isolated from patients of these outbreaks did not produce any known enterotoxin and did not carry the C. perfringens enterotoxin gene. However, the culture filtrates of these isolates induced the accumulation of fl...

Clostridium perfringens produces enteric diseases, generically called enterotoxemias, in sheep, goats, and other animals. This microorganism can be a normal inhabitant of the intestine of most animal species, including humans, but when the intestinal environment is altered by sudden changes in diet or other factors, C. perfringens proliferates and produces potent toxins that act locally or are ...

In vitro, Clostridium perfringens enterotoxin (CPE) binds to human ileal epithelium and induces morphological damage concurrently with reduced short-circuit current, transepithelial resistance, and net water absorption. CPE also binds to the human colon in vitro but causes only slight morphological and transport changes that are not statistically significant.

Siastatins A and B were isolated as part of a program designed to find Streptomyces-produced inhibitors of sialidase from Clostridium perfringens. Siastatin A was more effective than was siastatin B in the inhibition of sialidases prepared from Cl. perfringens and chicken chorioallantoic membrane. However, siastatin B was a stronger inhibitor of sialidases prepared from streptomyces and rat org...