Open AccessFunctional Characterization of a Redundant Plasmodium TRAP Family Invasin, TRAP-Like Protein, by Aldolase Binding and a Genetic Complementation Test
Author(s) -
Kirsten Heiß,
Hongtao Nie,
S. Kumar,
Thomas M. Daly,
Lawrence W. Bergman,
Kai Matuschewski
Publication year - 2008
Publication title -
eukaryotic cell
Language(s) - English
Resource type - Journals
eISSN - 1535-9778
pISSN - 1535-9786
DOI - 10.1128/ec.00089-08
Subject(s) - biology , complementation , aldolase a , trap (plumbing) , microbiology and biotechnology , plasmodium (life cycle) , microneme , actin , bacterial adhesin , transmembrane protein , genetics , apicomplexa , gene , parasite hosting , biochemistry , plasmodium falciparum , immunology , receptor , escherichia coli , environmental engineering , world wide web , computer science , malaria , engineering , phenotype , enzyme
Efficient and specific host cell entry is of exquisite importance for intracellular pathogens. Parasites of the phylumApicomplexa 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. AlthoughTLP is expressed in invasive stages, targeted gene disruption revealed a nonvital role during life cycle progression. This is the first genetic analysis ofTLP , encoding a redundant TRAP family invasin, in the malaria parasite.