The RhopH complex is transferred to the host cell cytoplasm following red blood cell invasion by Plasmodium falciparum.
The high-molecular mass rhoptry protein complex (PfRhopH), which comprises three distinct gene products, RhopH1, RhopH2, and RhopH3, is known to be secreted and transferred to the parasitophorous vacuole membrane upon invasion of a red blood cell by the malaria parasite Plasmodium falciparum. Here we show that the merozoite-acquired RhopH complex is also transferred to defined domains of the red blood cell cytoplasm, and possibly transiently associated with Maurer's clefts. This is the first report of trafficking in the host cell cytoplasm for P. falciparum rhoptry proteins secreted upon red blood cell invasion. Based on its newly identified sub-cellular location and the phenotype of RhopH1 mutants, we propose that the RhopH complex participate in the assembly of the cytoadherence complex.
Vincensini
Laetitia
L
Unité de Biologie des Interactions Hôte-Parasite, CNRS URA 2581 Institut Pasteur, 25-28 Rue du Dr Roux, Paris, France.
Fall
Gamou
G
Berry
Laurence
L
Blisnick
Thierry
T
Braun Breton
Catherine
C
D000818:Animals; D015153:Blotting, Western; D003593:Cytoplasm / Q000737:chemistry*; D004912:Erythrocytes / Q000469:parasitology*; D047468:Immunoprecipitation; D008856:Microscopy, Fluorescence; D010963:Plasmodium falciparum / Q000502:physiology*; D021381:Protein Transport; D015800:Protozoan Proteins / Q000378:metabolism*
D015800:Protozoan Proteins; C065352:rhoptry associated protein, Plasmodium