title: Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth parasite Fasciola hepatica.
abstract: A cDNA was isolated from a cDNA expression library using serum prepared against a high molecular mass fraction of Fasciola hepatica excretory-secretory products. The full-length cDNA encodes a member of the recently described peroxiredoxin antioxidant family. Peroxiredoxin could be the major hydrogen peroxide removing antioxidant in F. hepatica since this parasite does not express a catalase and expresses little glutathione peroxidase activity. This novel antioxidant may be involved in functions such as protection against reactive oxygen species (ROS) generated by metabolic processes and/or protection of the parasite against ROS released by immune effector cells.
authors.affiliation: School of Biological Sciences, Dublin City University, Ireland.
authors.forename: S
authors.initials: S
authors.lastname: McGonigle
authors.forename: G P
authors.initials: GP
authors.lastname: Curley
authors.forename: J P
authors.initials: JP
authors.lastname: Dalton
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000975:Antioxidants; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D018509:DNA, Helminth; D005210:Fasciola hepatica / Q000201:enzymology* / Q000235:genetics; D017238:Genes, Helminth; D015801:Helminth Proteins / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D054464:Peroxiredoxins; D017386:Sequence Homology, Amino Acid
chemical_list: D000975:Antioxidants; D018509:DNA, Helminth; D015801:Helminth Proteins; D010544:Peroxidases; C107443:peroxiredoxin, Fasciola hepatica; D054464:Peroxiredoxins