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A major part of virulence for Plasmodium falciparum malaria infection, the most lethal parasitic disease of humans, results from increased rigidity and adhesiveness of infected host red cells. These changes are caused by parasite proteins exported to the erythrocyte using novel trafficking machinery assembled in the host cell. To understand these unique(More)
Virulence of Plasmodium falciparum, the most lethal parasitic disease in humans, results in part from adhesiveness and increased rigidity of infected erythrocytes. Pf332 is trafficked to the parasite-infected erythrocyte via Maurer's clefts, structures for protein sorting and export in the host erythrocyte. This protein has a domain similar to the(More)
FIGURE S1: Structure-based residue conservation in PfNapL, yNAP-1, hSET and Vps75. Identical, well-conserved, semi-conserved residues are colored red, pink and grey respectively. Residues colored blue are not conserved amongst the 4 proteins. The sequence identity between these 4 proteins varies from 14 to 25%. FIGURE S2: Southern blot of attempted gene(More)
BACKGROUND Nucleosome assembly proteins (NAPs) are histone chaperones that are crucial for the shuttling and incorporation of histones into nucleosomes. NAPs participate in the assembly and disassembly of nucleosomes thus contributing to chromatin structure organization. The human malaria parasite Plasmodium falciparum contains two nucleosome assembly(More)
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