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Eukaryotic Cell, June 2008, p. 1062-1070, Vol. 7, No. 6
1535-9778/08/$08.00+0 doi:10.1128/EC.00089-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Parasitology, Heidelberg University School of Medicine, 69120 Heidelberg, Germany,1 Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, Pennsylvania 191292
Received 11 March 2008/ Accepted 14 April 2008
Efficient and specific host cell entry is of exquisite importance for intracellular pathogens. Parasites of the phylum Apicomplexa are highly motile and actively enter host cells. These functions are mediated by type I transmembrane invasins of the TRAP family that link an extracellular recognition event to the parasite actin-myosin motor machinery. We systematically tested potential parasite invasins for binding to the actin bridging molecule aldolase and complementation of the vital cytoplasmic domain of the sporozoite invasin TRAP. We show that the ookinete invasin CTRP and a novel, structurally related protein, termed TRAP-like protein (TLP), are functional members of the TRAP family. Although TLP is expressed in invasive stages, targeted gene disruption revealed a nonvital role during life cycle progression. This is the first genetic analysis of TLP, encoding a redundant TRAP family invasin, in the malaria parasite.
Published ahead of print on 25 April 2008.
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