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Proteomic analysis of glutathione transferases from the liver fluke parasite, Fasciola hepatica
Author(s) -
Chemale Gustavo,
Morphew Russell,
Moxon Joseph V.,
Morassuti Alessandra L.,
LaCourse E. James,
Barrett John,
Johnston David A.,
Brophy Peter M.
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200600499
Subject(s) - fasciola hepatica , biology , liver fluke , fasciola , hepatica , parasite hosting , glutathione s transferase , proteomics , proteome , fasciola gigantica , glutathione , microbiology and biotechnology , helminths , enzyme , genetics , immunology , biochemistry , gene , world wide web , computer science
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 .