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    A cathepsin L-like protease from Strongylus vulgaris: An orthologue of Caenorhabditis elegans CPL-1

    Nic An Ultaigh, Sinéad and Carolan, James C. and Britton, Collette and Murray, Linda and Ryan, Michael F. (2009) A cathepsin L-like protease from Strongylus vulgaris: An orthologue of Caenorhabditis elegans CPL-1. Experimental Parasitology, 121 (4). pp. 293-299. ISSN 0014-4894

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    Cathespin L-like proteases (CPLs), characterized from a wide range of helminths, are significant in helminth biology. For example, in Caenorhabditis elegans CPL is essential for embryogenesis. Here, we report a cathepsin L-like gene from three species of strongyles that parasitize the horse, and describe the isolation of a cpl gene (Sv-cpl-1) from Strongylus vulgaris, the first such from equine strongyles. It encodes a protein of 354 amino acids with high similarity to other parasitic Strongylida (90–91%), and C. elegans CPL-1 (87%), a member of the same Clade. As S. vulgaris cpl-1 rescued the embryonic lethal phenotype of the C. elegans cpl-1 mutant, these genes may be orthologues, sharing the same function in each species. Targeting Sv-CPL-1 might enable novel control strategies by decreasing parasite development and transmission.

    Item Type: Article
    Additional Information: The definitive version of this article is available at Ultaigh SN, Carolan JC, Britton C, Murray L, Ryan MF. 2009, 'A cathepsin L-like protease from Strongylus vulgaris: an orthologue of Caenorhabditis elegans CPL-1', Experimental Parasitology, vol. 121, no.4 pp. 293-299. DOI: 10.1016/j.exppara.2008.11.002
    Keywords: Nematode; Equine parasite; Strongylus vulgaris; Cathepsin L gene; C. elegans mutant rescue;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 7169
    Identification Number:
    Depositing User: James Carolan
    Date Deposited: 07 Jul 2016 11:43
    Journal or Publication Title: Experimental Parasitology
    Publisher: Elsevier
    Refereed: Yes
    Use Licence: This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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