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

Proteomic analysis of glutathione transferases from the liver fluke parasite, Fasciola hepatica
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.
Amino Acid Sequence, Animals, Electrophoresis, Gel, Two-Dimensional, Fasciola hepatica/enzymology, Glutathione Transferase/analysis, Molecular Sequence Data, Phylogeny, Proteomics, Sequence Alignment, Tandem Mass Spectrometry
1615-9853
6263-6373
Chemale, Gustavo
deb52338-3855-43f8-a23b-2598915a65f3
Morphew, Russell
7b52a65f-6187-4f1c-bd73-2666d391f1de
Moxon, Joseph V
2c91a060-8d5a-4bd9-80ef-792eef979304
Morassuti, Alessandra L
f1acca8e-8447-41f5-a5cd-3ca7a083bcb6
Lacourse, E James
a6e2e1d6-c2dc-45c5-98e7-e2d7bab664e2
Barrett, John
7be4eee2-535c-4d35-abf7-b30854af98cd
Johnston, David A
b41163c9-b9d2-425c-af99-2a357204014e
Brophy, Peter M
c14048b7-696e-497b-bc3c-38457f7e902d
Chemale, Gustavo
deb52338-3855-43f8-a23b-2598915a65f3
Morphew, Russell
7b52a65f-6187-4f1c-bd73-2666d391f1de
Moxon, Joseph V
2c91a060-8d5a-4bd9-80ef-792eef979304
Morassuti, Alessandra L
f1acca8e-8447-41f5-a5cd-3ca7a083bcb6
Lacourse, E James
a6e2e1d6-c2dc-45c5-98e7-e2d7bab664e2
Barrett, John
7be4eee2-535c-4d35-abf7-b30854af98cd
Johnston, David A
b41163c9-b9d2-425c-af99-2a357204014e
Brophy, Peter M
c14048b7-696e-497b-bc3c-38457f7e902d

Chemale, Gustavo, Morphew, Russell, Moxon, Joseph V, Morassuti, Alessandra L, Lacourse, E James, Barrett, John, Johnston, David A and Brophy, Peter M (2006) Proteomic analysis of glutathione transferases from the liver fluke parasite, Fasciola hepatica. Proteomics, 6 (23), 6263-6373. (doi:10.1002/pmic.200600499).

Record type: 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.

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More information

Published date: 1 December 2006
Keywords: Amino Acid Sequence, Animals, Electrophoresis, Gel, Two-Dimensional, Fasciola hepatica/enzymology, Glutathione Transferase/analysis, Molecular Sequence Data, Phylogeny, Proteomics, Sequence Alignment, Tandem Mass Spectrometry

Identifiers

Local EPrints ID: 468902
URI: http://eprints.soton.ac.uk/id/eprint/468902
ISSN: 1615-9853
PURE UUID: 501604ed-49be-479e-b1a2-f91a3a86304a
ORCID for David A Johnston: ORCID iD orcid.org/0000-0001-6703-6014

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Date deposited: 31 Aug 2022 16:59
Last modified: 17 Mar 2024 03:11

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Contributors

Author: Gustavo Chemale
Author: Russell Morphew
Author: Joseph V Moxon
Author: Alessandra L Morassuti
Author: E James Lacourse
Author: John Barrett
Author: David A Johnston ORCID iD
Author: Peter M Brophy

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