A novel calmodulin-like protein from the liver fluke, Fasciola hepatica

Sean L. Russell, Neil V. McFerran, Catherine M. Moore, Yvonne Tsang, Peter Glass, Elizabeth M. Hoey, Alan Trudgett, David J. Timson

    Research output: Contribution to journalArticlepeer-review


    An 18.2 kDa protein from the liver fluke, Fasciola hepatica has been identified and characterised. The protein shows strongest sequence similarity to egg antigen proteins from Schistosoma mansoni, Schistosoma japonicum and Clonorchis sinensis. The protein is predicted to adopt a calmodulin-like fold; it thus represents the third calmodulin-like protein to be characterised in F. hepatica and has been named FhCaM3. Compared to the classical calmodulin structure there are some variations. Most noticeably, the central, linker helix is disrupted by a cysteine residue. Alkaline native gel electrophoresis showed that FhCaM3 binds calcium ions. This binding event increases the ability of the protein to bind the hydrophobic fluorescent probe 8-anilinonaphthalene-1- sulphonate, consistent with an increase in surface hydrophobicity as seen in other calmodulins. FhCaM3 binds to the calmodulin antagonists trifluoperazine and W7, but not to the myosin regulatory light chain binding compound praziquantel. Immunolocalisation demonstrated that the protein is found in eggs and vitelline cells. Given the critical role of calcium ions in egg formation and hatching this suggests that FhCaM3 may play a role in calcium signalling in these processes. Consequently the antagonism of FhCaM3 may, potentially, offer a method for inhibiting egg production and thus reducing the spread of infection.

    Original languageEnglish
    Pages (from-to)2398-2406
    Number of pages9
    Issue number11
    Publication statusPublished - 1 Nov 2012


    • Calcium binding protein
    • Calmodulin
    • EF-hand
    • Fascioliasis
    • Trifluoperazine


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