Characterization of glutathione S-transferase and its immunodiagnostic potential for detecting Taenia multiceps

- The glutathione S-transferase was first located in Taenia multiceps by immunofluorescence.
- An enzyme-linked immunosorbent assay based on recombined glutathione S-transferase was established.
- The new method showed specificity of 92.8% and sensitivity of 90% in detecting antibodies in serum from Taenia multiceps infected animals.
- Glutathione S-transferase of Taenia multiceps has the potential to be used as a diagnostic antigen for Coenurosis.

Taenia multiceps is a widespread zoonotic tapeworm parasite which infects cloven-hoofed animals around the world. Animal infection with Coenurus cerebralis, the coenurus larvae of T. multiceps (Tm), is often fatal, which is a major cause of economic losses in stockbreeding. This study amplified the glutathione S-transferase (GST) gene from the total RNA of C. cerebralis. The resulting protein, Tm-GST, consisted of 201 amino acids, and had a predicted molecular mass of 23.1 kDa. Its amino acid sequence shares 77.61% similarity with Echinococcus granulosus GST. Recombinant Tm-GST (rTm-GST) was expressed in Escherichia coli. The protein reacted with serum from goats infected with T. multiceps. Immunofluorescence signals indicated that Tm-GST was largely localized in the parenchymatous area of adult T. multiceps; in addition, it was also apparent in the coenurus. An enzyme-linked immunosorbent assay based on rTm-GST showed specificity of 92.8% (13/14) and sensitivity of 90% (18/20) in detecting anti-GST antibodies in serum from naturally infected animals. This study suggests that Tm-GST has the potential to be used as a diagnostic antigen for Coenurosis.