Hostname: page-component-586b7cd67f-t8hqh Total loading time: 0 Render date: 2024-11-27T01:06:48.219Z Has data issue: false hasContentIssue false
  • English
  • Français

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

Published online by Cambridge University Press:  01 July 1997

S. McGONIGLE ,
G. P. CURLEY  and
J. P. DALTON
S. McGONIGLE
Affiliation:
School of Biological Sciences, Dublin City University, Dublin 9, Ireland
G. P. CURLEY
Affiliation:
School of Biological Sciences, Dublin City University, Dublin 9, Ireland
J. P. DALTON
Affiliation:
School of Biological Sciences, Dublin City University, Dublin 9, Ireland
Get access Rights & Permissions [Opens in a new window]

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.

Keywords

Fasciola hepaticatrematodeperoxiredoxinthiol-specific antioxidantantioxidants
Type
Research Article
Information
Parasitology , Volume 115 , Issue 1 , July 1997 , pp. 101 - 104
Copyright
1997 Cambridge University Press

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)