Characterisation of a β-tubulin gene from the liver fluke, Fasciola hepatica

Robinson, MW; Hoey, EM; Fairweather, I; Dalton, JP; McGonigle, S; Trudgett, A

Characterisation of a β-tubulin gene from the liver fluke, Fasciola hepatica

Robinson, MW

Hoey, EM Fairweather, I Dalton, JP McGonigle, S Trudgett, A

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Publication Type:: Journal Article
Citation:: International Journal for Parasitology, 2001, 31 (11), pp. 1264 - 1268
Issue Date:: 2001-08-29

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Field	Value	Language
dc.contributor.author	Robinson, MW https://orcid.org/0000-0001-7191-0034	en_US
dc.contributor.author	Hoey, EM	en_US
dc.contributor.author	Fairweather, I	en_US
dc.contributor.author	Dalton, JP	en_US
dc.contributor.author	McGonigle, S	en_US
dc.contributor.author	Trudgett, A	en_US
dc.date.issued	2001-08-29	en_US
dc.identifier.citation	International Journal for Parasitology, 2001, 31 (11), pp. 1264 - 1268	en_US
dc.identifier.issn	0020-7519	en_US
dc.identifier.uri	http://hdl.handle.net/10453/26086
dc.description.abstract	This study represents the first β-tubulin sequence from a trematode parasite, namely, the liver fluke, Fasciola hepatica. PCR of genomic DNA showed that at least one β-tubulin gene from F. hepatica contains no introns. A number of amino acids in the primary sequence of fluke tubulin are different from those described previously in various nematode species and the cestode, Echinococcus multilocularis. β-Tubulin is an important target for benzimidazole anthelmintics, although (with the exception of triclabendazole) they show limited activity against F. hepatica. The amino acid differences in fluke β-tubulin are discussed in relation to the selective toxicity of benzimidazoles against helminths and the mechanism of drug resistance. © 2001 Australian Society for Parasitology Inc. All rights reserved.	en_US
dc.relation.ispartof	International Journal for Parasitology	en_US
dc.relation.isbasedon	10.1016/S0020-7519(01)00240-5	en_US
dc.subject.classification	Mycology & Parasitology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Fasciola hepatica	en_US
dc.subject.mesh	Benzimidazoles	en_US
dc.subject.mesh	Tubulin	en_US
dc.subject.mesh	Anthelmintics	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Base Sequence	en_US
dc.subject.mesh	Drug Resistance	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Triclabendazole	en_US
dc.title	Characterisation of a β-tubulin gene from the liver fluke, Fasciola hepatica	en_US
dc.type	Journal Article
utslib.citation.volume	11	en_US
utslib.citation.volume	31	en_US
utslib.for	060502 Infectious Agents	en_US
utslib.for	060107 Enzymes	en_US
utslib.for	110803 Medical Parasitology	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	0608 Zoology	en_US
utslib.for	0707 Veterinary Sciences	en_US
pubs.embargo.period	Not known	en_US
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 Life Sciences
utslib.copyright.status	closed_access
pubs.issue	11	en_US
pubs.publication-status	Published	en_US
pubs.volume	31	en_US

Abstract:

This study represents the first β-tubulin sequence from a trematode parasite, namely, the liver fluke, Fasciola hepatica. PCR of genomic DNA showed that at least one β-tubulin gene from F. hepatica contains no introns. A number of amino acids in the primary sequence of fluke tubulin are different from those described previously in various nematode species and the cestode, Echinococcus multilocularis. β-Tubulin is an important target for benzimidazole anthelmintics, although (with the exception of triclabendazole) they show limited activity against F. hepatica. The amino acid differences in fluke β-tubulin are discussed in relation to the selective toxicity of benzimidazoles against helminths and the mechanism of drug resistance. © 2001 Australian Society for Parasitology Inc. All rights reserved.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/26086