Cloning and expression of C-terminal of Clostridium perfringens type A enterotoxin and its biological activity


Atieyeh Taherian Fard1 , Fariha Hasan, Mojgan Bandehpour , Nariman Mosaffa, Fatemeh Mashhadi Abbas, Abdul Hameed, Aamer Ali Shah and Bahram Kazemi

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 Claudine-expressing cells.

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