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

  • Chemale G
  • Morphew R
  • Moxon J
 et al. 
  • 41

    Readers

    Mendeley users who have this article in their library.
  • 33

    Citations

    Citations of this article.

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.

Author-supplied keywords

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

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text

Authors

  • Gustavo Chemale

  • Russell Morphew

  • Joseph V. Moxon

  • Alessandra L. Morassuti

  • E. James LaCourse

  • John Barrett

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free