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

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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.subject Animals, Cattle, Sheep, Fascioliasis, Sheep Diseases, Cathepsins, Cysteine Endopeptidases, Vaccines, Antigens, Helminth, Gene Expression, Intestines, Cathepsin L, Host-Parasite Interactions, Cattle Diseases, Fasciola hepatica, Animals, Antigens, Helminth, Cathepsin L, Cathepsins, Cattle, Cattle Diseases, Cysteine Endopeptidases, Fasciola hepatica, Fascioliasis, Gene Expression, Host-Parasite Interactions, Intestines, Sheep, Sheep Diseases, Vaccines, Helminths, Trematodes, Parasites, Cathepsins, Proteases, Vaccines, Immunology, Biochemistry, Mycology & Parasitology
dc.subject Animals; Cattle; Sheep; Fascioliasis; Sheep Diseases; Cathepsins; Cysteine Endopeptidases; Vaccines; Antigens, Helminth; Gene Expression; Intestines; Cathepsin L; Host-Parasite Interactions; Cattle Diseases; Fasciola hepatica; Animals; Antigens, Helminth; Cathepsin L; Cathepsins; Cattle; Cattle Diseases; Cysteine Endopeptidases; Fasciola hepatica; Fascioliasis; Gene Expression; Host-Parasite Interactions; Intestines; Sheep; Sheep Diseases; Vaccines; Helminths; Trematodes; Parasites; Cathepsins; Proteases; Vaccines; Immunology; Biochemistry; Mycology & Parasitology
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 030896 en_US
dc.personcode 0000021604 en_US
dc.personcode 995262 en_US
dc.personcode 0000021866 en_US
dc.personcode 0000020316 en_US
dc.personcode 0000024449 en_US
dc.personcode 00010696 en_US
dc.personcode 0000023163 en_US
dc.personcode 0000033399 en_US
dc.personcode 0000026108 en_US
dc.personcode 0000026356 en_US
dc.personcode 0000021869 en_US
dc.personcode 0000021870 en_US
dc.personcode 0000033731 en_US
dc.personcode 0000021873 en_US
dc.personcode 995261 en_US
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 Helminths; Trematodes; Parasites; Cathepsins; Proteases; Vaccines; Immunology; Biochemistry en_US
dc.description.keywords Self-assembled Monolayers
dc.description.keywords Containing Alkylthiolate Monolayers
dc.description.keywords Biotin Binding
dc.description.keywords Molecular Recognition
dc.description.keywords Indium-111-labeled Biotin
dc.description.keywords Subunit Association
dc.description.keywords Core Streptavidin
dc.description.keywords Wild-type
dc.description.keywords Avidin
dc.description.keywords Protein
dc.description.keywords Intestines
dc.description.keywords Animals
dc.description.keywords Cattle
dc.description.keywords Sheep
dc.description.keywords Fasciola hepatica
dc.description.keywords Fascioliasis
dc.description.keywords Cattle Diseases
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 Host-Parasite Interactions
dc.description.keywords Cathepsin L
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
dc.staffid 995261 en_US
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/Faculty of Science/School of Medical and Molecular Sciences
pubs.organisational-group /University of Technology Sydney/Strength - i3


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