Alteration in sporulation, enterotoxin production, and protein synthesis by Clostridium perfringens type A following heat shock.

Application of a heat shock (43 to 50 degrees C) applied early during the sporulation process of Clostridium perfringens delayed spore and enterotoxin production. Final levels of heat-resistant spores were similar to the control, but enterotoxin levels were reduced when the heat shock was applied at the third hour of incubation. The response of the microorganism to the heat shock was also examined by analysis of pulse-labeled proteins. Seven heat shock proteins (HSPs) associated with vegetative cells were identified by polyacrylamide gel electrophoresis. Most were localized mainly in the membrane, although one small protein was mostly present in the cytoplasm. Fewer HSPs were detected during sporulation. Two HSPs were immunologically related to the GroEL and DnaK HSPs from Lactobacillus lactis and Escherichia coli, respectively.