Figure 7.
Figure 7. Model of erythrocyte DRM rafts and their enrichment in the malarial vacuolar membrane. The uninfected erythrocyte membrane contains a dynamic milieu of generalized lipid domains (gray spheres) and raft microdomains (pink spheres) containing various proteins. Some proteins partition heavily into raft domains (ie, flotillins), while others are only minimally present in rafts (ie, band 3, Glut1). During malaria infection, merozoite-stage parasites invade erythrocytes to reside in a membrane-bound parasitophorous vacuole. The PVM becomes selectively cholesterol-enriched, and 10 of the known raft proteins are internalized to the PVM (flotillin-1 and -2, Gαs, β2-AR, AQP1, Duffy, CD55, CD58, CD59, scramblase). Most of the abundant erythrocyte membrane proteins are not internalized to the PVM (ie, glycophorins A and C, cytoskeleton-associated band 3, and others). The lower left inset shows the perspective of the model, which depicts a whole infected erythrocyte and a magnified view through the plasma membrane and PVM of a malaria-infected erythrocyte. Because the PVM is formed by invagination of the plasma membrane, proteins that are cytoplasmically oriented in uninfected cells remain so upon infection; protein structures exposed to the extracellular space face the vacuolar space upon infection. 4.1 indicates band 4.1.

Model of erythrocyte DRM rafts and their enrichment in the malarial vacuolar membrane. The uninfected erythrocyte membrane contains a dynamic milieu of generalized lipid domains (gray spheres) and raft microdomains (pink spheres) containing various proteins. Some proteins partition heavily into raft domains (ie, flotillins), while others are only minimally present in rafts (ie, band 3, Glut1). During malaria infection, merozoite-stage parasites invade erythrocytes to reside in a membrane-bound parasitophorous vacuole. The PVM becomes selectively cholesterol-enriched, and 10 of the known raft proteins are internalized to the PVM (flotillin-1 and -2, Gαs, β2-AR, AQP1, Duffy, CD55, CD58, CD59, scramblase). Most of the abundant erythrocyte membrane proteins are not internalized to the PVM (ie, glycophorins A and C, cytoskeleton-associated band 3, and others). The lower left inset shows the perspective of the model, which depicts a whole infected erythrocyte and a magnified view through the plasma membrane and PVM of a malaria-infected erythrocyte. Because the PVM is formed by invagination of the plasma membrane, proteins that are cytoplasmically oriented in uninfected cells remain so upon infection; protein structures exposed to the extracellular space face the vacuolar space upon infection. 4.1 indicates band 4.1.

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