Remodeling of human red cells infected with Plasmodium falciparum and the impact of PHIST proteins

In an infected erythrocyte (iRBC), renovation and decoration are crucial for malarial parasite survival, pathogenesis and reproduction. Host cell remodeling is mediated by an array of diverse parasite-encoded export proteins that traffic within iRBC. These remodeling proteins extensively modify the membrane and cytoskeleton of iRBC and help in formation of parasite-induced novel organelles such as 'Maurer's Cleft (MC), tubulovesicular network (TVN) and parasitophorous vacuole membrane (PVM) inside the iRBC. The genome sequence of Plasmodium falciparum shows expansion of export proteins, which suggests a complex requirement of these export proteins for specific pathogenesis and erythrocyte remodeling. Plasmodium helical intersperse sub-telomeric (PHIST) is a family of seventy-two small export proteins and many of its recently discovered functional characteristics suggest an intriguing putative role in modification of an iRBC. This review highlights the recent advances in parasite genomics, proteomics, and cell biology studies unraveling the host cell modification; providing a speculation on the impact of PHIST proteins in modification of the iRBC.