Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines.

DSpace/Manakin Repository

Search OPUS

Advanced Search


My Account

Show simple item record

dc.contributor.author Dalton, JP
dc.contributor.author Neill, SO
dc.contributor.author Stack, C
dc.contributor.author Collins, P
dc.contributor.author Walshe, A
dc.contributor.author Sekiya, M
dc.contributor.author Doyle, S
dc.contributor.author Mulcahy, G
dc.contributor.author Hoyle, D
dc.contributor.author Khaznadji, E
dc.contributor.author Moiré, N
dc.contributor.author Brennan, G
dc.contributor.author Mousley, A
dc.contributor.author Kreshchenko, N
dc.contributor.author Maule, AG
dc.contributor.author Donnelly, SM
dc.date.accessioned 2010-05-28T09:46:12Z
dc.date.issued 2003-09
dc.identifier.citation International journal for parasitology, 2003, 33 (11), pp. 1173 - 1181
dc.identifier.issn 0020-7519
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/8903
dc.description.abstract Fasciola hepatica secretes cathepsin L proteases that facilitate the penetration of the parasite through the tissues of its host, and also participate in functions such as feeding and immune evasion. The major proteases, cathepsin L1 (FheCL1) and cathepsin L2 (FheCL2) are members of a lineage that gave rise to the human cathepsin Ls, Ks and Ss, but while they exhibit similarities in their substrate specificities to these enzymes they differ in having a wider pH range for activity and an enhanced stability at neutral pH. There are presently 13 Fasciola cathepsin L cDNAs deposited in the public databases representing a gene family of at least seven distinct members, although the temporal and spatial expression of each of these members in the developmental stage of F. hepatica remains unclear. Immunolocalisation and in situ hybridisation studies, using antibody and DNA probes, respectively, show that the vast majority of cathepsin L gene expression is carried out in the epithelial cells lining the parasite gut. Within these cells the enzyme is packaged into secretory vesicles that release their contents into the gut lumen for the purpose of degrading ingested host tissue and blood. Liver flukes also express a novel multi-domain cystatin that may be involved in the regulation of cathepsin L activity. Vaccine trials in both sheep and cattle with purified native FheCL1 and FheCL2 have shown that these enzymes can induce protection, ranging from 33 to 79%, to experimental challenge with metacercariae of F. hepatica, and very potent anti-embryonation/hatch rate effects that would block parasite transmission. In this article we review the vaccine trials carried out over the past 8 years, the role of antibody and T cell responses in mediating protection and discuss the prospects of the cathepsin Ls in the development of first generation recombinant liver fluke vaccines.
dc.format Print
dc.language eng
dc.relation.isbasedon 10.1016/s0020-7519(03)00171-1
dc.title Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines.
dc.type Journal Article
dc.parent International journal for parasitology
dc.journal.volume 11
dc.journal.volume 33
dc.journal.number 11 en_US
dc.publocation Oxford, UK en_US
dc.identifier.startpage 1173 en_US
dc.identifier.endpage 1181 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 0707 Veterinary Sciences
dc.personcode 995262
dc.personcode 995261
dc.personcode 030896
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.location.activity ISI:000221022400037
dc.description.keywords Animals
dc.description.keywords Cattle
dc.description.keywords Sheep
dc.description.keywords Fascioliasis
dc.description.keywords Sheep Diseases
dc.description.keywords Cathepsins
dc.description.keywords Cysteine Endopeptidases
dc.description.keywords Vaccines
dc.description.keywords Antigens, Helminth
dc.description.keywords Gene Expression
dc.description.keywords Intestines
dc.description.keywords Cathepsin L
dc.description.keywords Host-Parasite Interactions
dc.description.keywords Cattle Diseases
dc.description.keywords Fasciola hepatica
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 false
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)
utslib.collection.history Closed (ID: 3)

Files in this item

This item appears in the following Collection(s)

Show simple item record