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dc.contributor.authorHeaslip, Aoife T.
dc.contributor.authorLeung, Jacqueline M.
dc.contributor.authorCarey, Kimberly L.
dc.contributor.authorCatti, Federica
dc.contributor.authorWarshaw, David M.
dc.contributor.authorWestwood, Nicholas J.
dc.contributor.authorBallif, Bryan A.
dc.contributor.authorWard, Gary E.
dc.identifier.citationHeaslip , A T , Leung , J M , Carey , K L , Catti , F , Warshaw , D M , Westwood , N J , Ballif , B A & Ward , G E 2010 , ' A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity ' , PLoS Pathogens , vol. 6 , no. 1 , e1000720 .
dc.identifier.otherPURE: 22871166
dc.identifier.otherPURE UUID: d354ecd1-922c-4610-87aa-bd4eedd1bf73
dc.identifier.otherWOS: 000274227100011
dc.identifier.otherScopus: 77649199675
dc.identifier.otherORCID: /0000-0003-0630-0138/work/56424161
dc.description.abstractToxoplasma gondii is an obligate intracellular parasite that enters cells by a process of active penetration. Host cell penetration and parasite motility are driven by a myosin motor complex consisting of four known proteins: TgMyoA, an unconventional Class XIV myosin; TgMLC1, a myosin light chain; and two membrane-associated proteins, TgGAP45 and TgGAP50. Little is known about how the activity of the myosin motor complex is regulated. Here, we show that treatment of parasites with a recently identified small-molecule inhibitor of invasion and motility results in a rapid and irreversible change in the electrophoretic mobility of TgMLC1. While the precise nature of the TgMLC1 modification has not yet been established, it was mapped to the peptide Val46-Arg59. To determine if the TgMLC1 modification is responsible for the motility defect observed in parasites after compound treatment, the activity of myosin motor complexes from control and compound-treated parasites was compared in an in vitro motility assay. TgMyoA motor complexes containing the modified TgMLC1 showed significantly decreased motor activity compared to control complexes. This change in motor activity likely accounts for the motility defects seen in the parasites after compound treatment and provides the first evidence, in any species, that the mechanical activity of Class XIV myosins can be modulated by posttranslational modifications to their associated light chains.
dc.relation.ispartofPLoS Pathogensen
dc.rights© 2010 Heaslip et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectQD Chemistryen
dc.titleA small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activityen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.description.statusPeer revieweden

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