Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth parasite Fasciola hepatica

Parasitology. 1997 Jul:115 ( Pt 1):101-4. doi: 10.1017/s0031182097001170.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antioxidants*
  • Base Sequence
  • Cattle
  • Cloning, Molecular
  • DNA, Helminth
  • Fasciola hepatica / enzymology*
  • Fasciola hepatica / genetics
  • Genes, Helminth*
  • Helminth Proteins / genetics*
  • Humans
  • Molecular Sequence Data
  • Peroxidases / chemistry
  • Peroxidases / genetics*
  • Peroxidases / metabolism
  • Peroxiredoxins
  • Sequence Homology, Amino Acid

Substances

  • Antioxidants
  • DNA, Helminth
  • Helminth Proteins
  • Peroxidases
  • peroxiredoxin, Fasciola hepatica
  • Peroxiredoxins

Associated data

  • GENBANK/U88577