Eukaryotic Cell doi:10.1128/EC.00089-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
Functional characterization of a redundant Plasmodium TRAP-family invasin, TRAP-like protein (TLP), by aldolase binding and a genetic complementation test
Kirsten Heiss,
Hui Nie,
Sumit Kumar,
Thomas M. Daly,
Lawrence W. Bergman*,
and
Kai Matuschewski*
Department of Parasitology, Heidelberg University School of Medicine, 69120 Heidelberg, Germany; Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129
* To whom correspondence should be addressed. Email:
Lawrence.Bergman{at}DrexelMed.edu. Kai.Matuschewski{at}med.uni-heidelberg.de.
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Abstract |
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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 non-vital role during life cycle progression. This is the first genetic analysis of TLP, a redundant TRAP-family invasin, in the malaria parasite.
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