A unique thioredoxin of the parasitic nematode Haemonchus contortus with glutaredoxin activity

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dc.contributor.author Sotirchos, IM
dc.contributor.author Hudson, AL
dc.contributor.author Ellis, J
dc.contributor.author Davey, MW
dc.date.accessioned 2010-05-28T09:43:21Z
dc.date.issued 2009-03-01
dc.identifier.citation Free Radical Biology and Medicine, 2009, 46 (5), pp. 579 - 585
dc.identifier.issn 0891-5849
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/8462
dc.description.abstract The dependency of parasites on the cellular redox systems has led to their investigation as novel drug targets. Defence against oxidative damage is through the thioredoxin and glutathione systems. The classic thioredoxin is identified by the active site Cys-Gly-Pro-Cys (CGPC). Here we describe the identification of a unique thioredoxin in the parasitic nematode, Haemonchus contortus. This thioredoxin-related protein, termed HcTrx5, has an arginine in its active site (Cys-Arg-Ser-Cys; CRSC) that is not found in any other organism. Recombinant HcTrx5 was able to reduce the disulfide bond in insulin, and be regenerated by mammalian thioredoxin reductase with a Km 2.19 ± 1.5 μM, similar to the classic thioredoxins. However, it was also able to reduce insulin when glutathione and glutathione reductase replaced the thioredoxin reductase. When coupled with H. contortus peroxiredoxin, HcTrx5 was active using either the thioredoxin reductase or the glutathione and glutathione reductase. HcTrx5 is expressed through the life cycle, with highest expression in the adult stage. The unique activity of this thioredoxin makes it a potential drug target for the control of this parasite. © 2008 Elsevier Inc. All rights reserved.
dc.language eng
dc.relation.isbasedon 10.1016/j.freeradbiomed.2008.11.009
dc.title A unique thioredoxin of the parasitic nematode Haemonchus contortus with glutaredoxin activity
dc.type Journal Article
dc.parent Free Radical Biology and Medicine
dc.journal.volume 5
dc.journal.volume 46
dc.journal.number en_US
dc.journal.number 5 en_US
dc.publocation Switzerland en_US
dc.identifier.startpage 579 en_US
dc.identifier.endpage 585 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 0707 Veterinary Sciences
dc.personcode 880134
dc.personcode 030905
dc.personcode 910945
dc.percentage 100 en_US
dc.classification.name Veterinary Sciences en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords Drug target
dc.description.keywords Functional characterisation
dc.description.keywords Glutaredoxin
dc.description.keywords Haemonchus contortus
dc.description.keywords Nematode
dc.description.keywords Thioredoxin
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - i3
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)
utslib.collection.history Closed (ID: 3)
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)

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