CLONING OF PEROXIREDOXIN, A NOVEL ANTIOXIDANT ENZYME, FROM THE HELMINTH PARASITE FASCIOLA-HEPATICA

A cDNA was isolated from a cDNA expression library using serum prepare d against a high molecular mass fraction of Fasciola hepatica excretor y-secretory products. The full-length cDNA encodes a member of the rec ently described peroxiredoxin antioxidant family. Peroxiredoxin could be the major hydrogen peroxide removing antioxidant in F. hepatica sin ce this parasite does not express a catalase and expresses little glut athione peroxidase activity. This novel antioxidant may be involved in functions such as protection against reactive oxygen species (ROS) ge nerated by metabolic processes and/or protection of the parasite again st ROS released by immune effector cells.