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Background  Copper is an essential catalytic co-factor for metabolically important cellular enzymes, such as cytochrome-c oxidase. Eukaryotic cells acquire copper through a copper transport protein and distribute intracellular copper using molecular chaperones. The copper chelator, neocuproine, inhibits  Plasmodium falciparum  ring-to-trophozoite transition  in vitro , indicating a copper requirement for malaria parasite development. How the malaria parasite acquires or secretes copper still remains to be fully elucidated.    Methods  PlasmoDB was searched for sequences corresponding to candidate  P. falciparum  copper-requiring proteins. The amino terminal domain of a putative  P. falciparum  copper transport protein was cloned and expressed as a maltose binding fusion protein. The copper binding ability of this protein was examined. Copper transport protein-specific anti-peptide antibodies were generated in chickens and used to establish native protein localization in  P. falciparum  parasites by immunofluorescence microscopy.    Results  Six  P. falciparum  copper-requiring protein orthologs and a candidate  P. falciparum  copper transport protein (PF14_0369), containing characteristic copper transport protein features, were identified in PlasmoDB. The recombinant amino terminal domain of the transport protein bound reduced copper  in vitro  and within  Escherichia coli  cells during recombinant expression. Immunolocalization studies tracked the copper binding protein translocating from the erythrocyte plasma membrane in early ring stage to a parasite membrane as the parasites developed to schizonts. The protein appears to be a PEXEL-negative membrane protein.    Conclusion   Plasmodium falciparum  parasites express a native protein with copper transporter characteristics that binds copper  in vitro . Localization of the protein to the erythrocyte and parasite plasma membranes could provide a mechanism for the delivery of novel anti-malarial compounds.

A Plasmodium falciparum copper-binding membrane protein with copper transport motifs