Fasciola hepatica expresses multiple α- and β-tubulin isotypes

Ryan, LA; Hoey, E; Trudgett, A; Fairweather, I; Fuchs, M; Robinson, MW; Chambers, E; Timson, DJ; Ryan, E; Feltwell, T; Ivens, A; Bentley, G; Johnston, D

Fasciola hepatica expresses multiple α- and β-tubulin isotypes

Ryan, LA Hoey, E Trudgett, A Fairweather, I Fuchs, M Robinson, MW

Chambers, E Timson, DJ Ryan, E Feltwell, T Ivens, A Bentley, G Johnston, D

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Publication Type:: Journal Article
Citation:: Molecular and Biochemical Parasitology, 2008, 159 (1), pp. 73 - 78
Issue Date:: 2008-05-01

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Field	Value	Language
dc.contributor.author	Ryan, LA	en_US
dc.contributor.author	Hoey, E	en_US
dc.contributor.author	Trudgett, A	en_US
dc.contributor.author	Fairweather, I	en_US
dc.contributor.author	Fuchs, M	en_US
dc.contributor.author	Robinson, MW https://orcid.org/0000-0001-7191-0034	en_US
dc.contributor.author	Chambers, E	en_US
dc.contributor.author	Timson, DJ	en_US
dc.contributor.author	Ryan, E	en_US
dc.contributor.author	Feltwell, T	en_US
dc.contributor.author	Ivens, A	en_US
dc.contributor.author	Bentley, G	en_US
dc.contributor.author	Johnston, D	en_US
dc.date.available	2008-02-06	en_US
dc.date.issued	2008-05-01	en_US
dc.identifier.citation	Molecular and Biochemical Parasitology, 2008, 159 (1), pp. 73 - 78	en_US
dc.identifier.issn	0166-6851	en_US
dc.identifier.uri	http://hdl.handle.net/10453/12538
dc.description.abstract	We have identified five α-tubulin and six β-tubulin isotypes that are expressed in adult Fasciola hepatica. Amino acid sequence identities ranged between 72 and 95% for fluke α-tubulin and between 65 and 97% for β-tubulin isotypes. Nucleotide sequence identity ranged between 68-77% and 62-80%, respectively, for their coding sequences. Phylogenetic analysis indicated that two of the α-tubulins and two of the β-tubulins were distinctly divergent from the other trematode and nematode tubulin sequences described in this study, whereas the other isotypes segregated within the trematode clades. With regard to the proposed benzimidazole binding site on β-tubulin, three of the fluke isotypes had tyrosine at position 200 of β-tubulin, two had phenylalanine and one had leucine. All had phenylalanine at position 167 and glutamic acid at position 198. When isotype RT-PCR fragment sequences were compared between six individual flukes from the susceptible Cullompton isolate and from seven individual flukes from the two resistant isolates, Sligo and Oberon, these residues were conserved. © 2008 Elsevier B.V. All rights reserved.	en_US
dc.relation.ispartof	Molecular and Biochemical Parasitology	en_US
dc.relation.isbasedon	10.1016/j.molbiopara.2008.02.001	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	Sequence Analysis, DNA	en_US
dc.subject.mesh	Phylogeny	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Drug Resistance	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.title	Fasciola hepatica expresses multiple α- and β-tubulin isotypes	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	159	en_US
utslib.for	0707 Veterinary Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	07 Agricultural and Veterinary Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
dc.location.activity	Netherlands
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
utslib.copyright.status	closed_access
pubs.issue	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	159	en_US

Abstract:

We have identified five α-tubulin and six β-tubulin isotypes that are expressed in adult Fasciola hepatica. Amino acid sequence identities ranged between 72 and 95% for fluke α-tubulin and between 65 and 97% for β-tubulin isotypes. Nucleotide sequence identity ranged between 68-77% and 62-80%, respectively, for their coding sequences. Phylogenetic analysis indicated that two of the α-tubulins and two of the β-tubulins were distinctly divergent from the other trematode and nematode tubulin sequences described in this study, whereas the other isotypes segregated within the trematode clades. With regard to the proposed benzimidazole binding site on β-tubulin, three of the fluke isotypes had tyrosine at position 200 of β-tubulin, two had phenylalanine and one had leucine. All had phenylalanine at position 167 and glutamic acid at position 198. When isotype RT-PCR fragment sequences were compared between six individual flukes from the susceptible Cullompton isolate and from seven individual flukes from the two resistant isolates, Sligo and Oberon, these residues were conserved. © 2008 Elsevier B.V. All rights reserved.

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http://hdl.handle.net/10453/12538