Fasciola hepatica expresses multiple α- and β-tubulin isotypes

Louise A. Ryan, Elizabeth Hoey, Alan Trudgett, Ian Fairweather, Marc Fuchs, Mark W. Robinson, Emma Chambers, David J. Timson, Eimear Ryan, Theresa Feltwell, Al Ivens, Geoffrey Bentley, David Johnston

    Research output: Contribution to journalArticlepeer-review


    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.

    Original languageEnglish
    Pages (from-to)73-78
    Number of pages6
    JournalMolecular and Biochemical Parasitology
    Issue number1
    Publication statusPublished - 1 May 2008


    • Drug resistance
    • Fasciola hepatica
    • Isotypes
    • Trematode
    • Tubulin


    Dive into the research topics of 'Fasciola hepatica expresses multiple α- and β-tubulin isotypes'. Together they form a unique fingerprint.

    Cite this