Proteomic analysis of glutathione transferases from the liver fluke parasite, Fasciola hepatica

Authors Organisations
Type Article
Original languageEnglish
Pages (from-to)6263-6273
Number of pages11
JournalProteomics
Volume6
Issue number23
Early online date31 Oct 2006
DOI
Publication statusPublished - 23 Dec 2006
Links
View graph of relations
Citation formats

Abstract

The parasite Fasciola hepatica causes major global disease of livestock, with increasing reports of human infection. Vaccine candidates with varying protection rates have been identified by pre-genomic approaches. As many candidates are part of protein superfamilies, sub-proteomics offers new possibilities to systematically reveal the relative importance of individual family proteins to vaccine formulations within populations. The superfamily glutathione transferase (GST) from liver fluke has phase II detoxification and housekeeping roles, and has been shown to contain protective vaccine candidates. GST were purified from cytosolic fractions of adult flukes using glutathione- and S-hexylglutathione-agarose, separated by 2-DE, and identified by MS/MS, with the support of a liver fluke EST database. All previously described F. hepatica GST isoforms were identified in 2-DE. Amongst the isoforms mapped by 2-DE, a new GST, closely related to the Sigma class enzymes is described for the first time in the liver fluke. We also describe cDNA encoding putative Omega class GST in F. hepatica.

Keywords

  • 2-DE, F. hepatica, Glutathione transferases, Omega, Sigma