Pexel/VTS: a protein-export motif in erythrocytes infected with malaria parasites.
The trafficking of proteins from the malaria parasite into the erythrocyte host has an important role in both the adaptation by the parasite of its immediate environment and the pathophysiology of disease. The molecular basis of these trafficking processes, particularly export from the parasitophorous vacuole (PV), is poorly understood and a matter of some controversy. In this article, we highlight two recent, independent reports that have provided new insights into protein translocation across the PV membrane, characterizing a novel signalling motif as a key signature in cataloguing the parasite secretome.
Horrocks
Paul
P
Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DS, UK. horrocks@hammer.imm.ox.ac.uk
Muhia
David
D
D020816:Amino Acid Motifs; D000818:Animals; D003600:Cytosol / Q000378:metabolism / Q000469:parasitology; D004910:Erythrocyte Membrane / Q000378:metabolism / Q000469:parasitology; D004912:Erythrocytes / Q000469:parasitology*; D006790:Host-Parasite Interactions; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*; D015800:Protozoan Proteins / Q000378:metabolism*; D022142:Secretory Vesicles / Q000378:metabolism / Q000469:parasitology
D008565:Membrane Proteins; D015800:Protozoan Proteins