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Brief Report |
Correspondence to: Robert Ménard, Department of Pathology, Division of Immunology, New York University School of Medicine, 550 First Avenue, New York, NY 10016. Tel:(212) 263-7870 Fax:(212) 263-8179 E-mail:menarr01{at}mcrcr6.med.nyu.edu.
Most Apicomplexan parasites, including the human pathogens Plasmodium, Toxoplasma, and Cryptosporidium, actively invade host cells and display gliding motility, both actions powered by parasite microfilaments. In Plasmodium sporozoites, thrombospondin-related anonymous protein (TRAP), a member of a group of Apicomplexan transmembrane proteins that have common adhesion domains, is necessary for gliding motility and infection of the vertebrate host. Here, we provide genetic evidence that TRAP is directly involved in a capping process that drives both sporozoite gliding and cell invasion. We also demonstrate that TRAP-related proteins in other Apicomplexa fulfill the same function and that their cytoplasmic tails interact with homologous partners in the respective parasite. Therefore, a mechanism of surface redistribution of TRAP-related proteins driving gliding locomotion and cell invasion is conserved among Apicomplexan parasites.
Key Words: gliding motility, cell invasion, Apicomplexan parasites, thrombospondin-related anonymous protein, micronemal protein 2
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