Structural highlights
FunctionPublication Abstract from PubMedThrombospondin-related anonymous protein (TRAP), localized in the micronemes and on the surface of sporozoites of infamous malaria parasite Plasmodium, is a key molecule upon infection of mammalian host hepatocytes and invasion of mosquito salivary glands. TRAP contains two adhesive domains responsible for host cell recognition and invasion, and is known to be essential for infectivity. Here we report high resolution crystal structures of the A domain of Plasmodium falciparum TRAP with and without bound Mg2+. The structure reveals a von Willebrand factor A (vWA)-like fold and a functional metal ion-dependent adhesion site (MIDAS), as well as a potential heparan sulphate binding site. Site-directed mutagenesis and cell attachment assays were used to investigate the functional roles of discovered surface epitopes. The reported structures are the first determined for a complete vWA domain of parasitic origin, highlighting unique features among homologous domains from other proteins characterized hitherto. Some of these are conserved among Plasmodiae exclusively, while others may be common to apicomplexan organisms in general. Structure of Plasmodium falciparum Thrombospondin-Related Anonymous Protein (TRAP) A domain highlights distinct features in apicomplexan von Willebrand Factor A homologues.,Pihlajamaa T, Kajander T, Knuuti J, Horkka K, Sharma A, Permi P Biochem J. 2013 Jan 15. PMID:23317521[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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