Proteomic analysis of glutathione transferases from the liver fluke parasite, Fasciola hepatica.
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.
Chemale
Gustavo
G
School of Biological Sciences, University of Liverpool, Liverpool, UK. g.chemale@liverpool.ac.uk
Morphew
Russell
R
Moxon
Joseph V
JV
Morassuti
Alessandra L
AL
Lacourse
E James
EJ
Barrett
John
J
Johnston
David A
DA
Brophy
Peter M
PM
D000595:Amino Acid Sequence; D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D005210:Fasciola hepatica / Q000201:enzymology*; D005982:Glutathione Transferase / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010802:Phylogeny; D040901:Proteomics; D016415:Sequence Alignment; D053719:Tandem Mass Spectrometry
D005982:Glutathione Transferase