Pathogenic clostridia produce exocellular toxins that resemble lipoteichoic acid and are described as
super antigens. These toxins stimulate T-cell receptor-carrying lymphocytes in peripheral blood and
have been used to study immunodeficiency diseases and cancers. The CPE C-terminal region from one
of the local type A strain was cloned in the pET32a vector its expression induced with IPTG. The
expressed protein was purified by Ni-NTA affinity chromatography and tested for biological activity with
Vero cells assay. This region of Clostridium perfringens enterotoxin (CPE) has a predominant ligandbinding
activity. In the present study, the biological activity of the C-terminal region of local purified
CPE came under study with Vero cell assay, guinea pig skin test and mouse test to evaluate for future
use as a therapeutic purpose. The result of this study showed that, the study’s local purified C-CPE had
cytotoxic activity in Vero cells even at the minimum dilution of 0.625 ng after a 4-h incubation period. It
caused transient increase in capillary permeability in guinea pigs. C-CPE did not have systemic effect
on Balb/c mice. The use of the C-CPE peptide may provide a novel way to target drugs to Claudineexpressing
cells.
