Functional and biophysical analyses of the class XIV Toxoplasma gondii Myosin D

Herm-Gotz, A. and Delbac, F. and Weiss, S. and Nyitrai, M. and Stratmann, R. and Tomavo, S. and Sibley, L.D. and Geeves, M.A. and Soldati, D. (2006) Functional and biophysical analyses of the class XIV Toxoplasma gondii Myosin D. Journal of Muscle Research and Cell Motility, 27 (2). pp. 139-51. ISSN 01424319. (The full text of this publication is not available from this repository)

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Abstract

The obligate intracellular parasite Toxoplasma gondii uses gliding motility to migrate across the biological barriers of the host and to invade cells. This unique form of locomotion requires an intact actin cytoskeleton and involves at least one motor protein (TgMyoA) that belongs to the class XIV of the myosin superfamily. TgMyoA is anchored in the inner membrane complex and is essential for the gliding motion, host cell invasion and egress of T. gondii tachyzoites. TgMyoD is the smallest T. gondii myosin and is structurally very closely related to TgMyoA. We show here that TgMyoD exhibits similar transient kinetic properties as the fast single-headed TgMyoA. To determine if TgMyoD also contributes to parasite gliding motility, the TgMyoD gene was disrupted by double homologous recombination. In contrast to TgMyoA, TgMyoD gene is dispensable for tachyzoite propagation and motility. Parasites lacking TgMyoD glide normally and their virulence is not compromised in mice. The fact that TgMyoD is predominantly expressed in bradyzoites explains the absence of a phenotype observed with myodko in tachyzoites and does not exclude a role of this motor in gliding that would be restricted to the cyst forming but nevertheless motile stage of the parasite.

Item Type: Article
Additional information: 0142-4319 (Print) Journal Article
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Michael Geeves
Date Deposited: 16 Mar 2009 16:31
Last Modified: 16 Mar 2009 16:36
Resource URI: http://kar.kent.ac.uk/id/eprint/13212 (The current URI for this page, for reference purposes)
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