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A more recent version of this article appeared on February 24, 2006
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M509807200v1
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Papers In Press, published online ahead of print December 1, 2005
J. Biol. Chem, 10.1074/jbc.M509807200
Submitted on September 7, 2005
Revised on November 28, 2005
Accepted on December 1, 2005

A conserved molecular motor drives cell invasion and gliding motility across malaria lifecycle stages and other apicomplexan parasites

Jake Baum, Dave Richard, Julie Healer, Melanie Rug, Zita Krnajski, Tim-Wolf Gilberger, Judith L. Green, Anthony A. Holder, and Alan F. Cowman

Dept. of Infection and Immunity, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3500

Corresponding Author: cowman{at}wehi.edu.au

Apicomplexan parasites constitute one of the most significant groups of pathogens infecting humans and animals. The liver stage sporozoites of Plasmodium spp. and tachyzoites of Toxoplasma gondii, the causative agents of malaria and toxoplasmosis respectively, use a unique mode of locomotion termed gliding motility to invade host cells and cross cell-substrates. This amoeboid-like movement uses a parasite adhesin from the thrombospondin-related-anonymous-protein (TRAP) family and a set of proteins linking the extracellular adhesin, via an actin-myosin motor, to the inner-membrane complex. The Plasmodium blood stage merozoite, however, does not exhibit gliding motility. Here we show that homologues of the key proteins that make up the motor complex, including the recently identified glideosome associated proteins (GAP) 45 and GAP50, are present in P. falciparum merozoites and appear to function in erythrocyte invasion. Furthermore, we identify a merozoite TRAP-homologue, termed MTRAP, a micronemal protein that shares key features with TRAP, including a thrombospondin repeat domain, a putative rhomboid-protease cleavage site and a cytoplasmic tail that, in vitro, binds the actin-binding protein aldolase. Analysis of other parasite genomes shows that the components of this motor complex are conserved across diverse Apicomplexan genera. Conservation of the motor complex suggests a common molecular mechanism underlies all Apicomplexan motility, which given its unique properties, highlights a number of novel targets for drug-intervention to treat major diseases of humans and livestock.


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