@article{oai:nagasaki-u.repo.nii.ac.jp:00005744,
 author = {Prajapati, Surendra Kumar and Culleton, Richard and Singh, Om Prakash},
 issue = {12},
 journal = {Parasitology},
 month = {Oct},
 note = {Erythrocytes are extensively remodelled by the malaria parasite following invasion of the cell. Plasmodium falciparum encodes numerous virulence-associated and host-cell remodelling proteins that are trafficked to the cytoplasm, the cell membrane and the surface of the infected erythrocyte. The export of soluble proteins relies on a sequence directing entry into the secretory pathways in addition to an export signal. The export signal consisting of five amino acids is termed the Plasmodium export element (PEXEL) or the vacuole transport signal (VTS). Genome mining studies have revealed that PEXEL/VTS carrying protein families have expanded dramatically in P. falciparum compared with other malaria parasite species, possibly due to lineage-specific expansion linked to the unique requirements of P. falciparum for host-cell remodelling. The functional characterization of such genes and gene families may reveal potential drug targets that could inhibit protein trafficking in infected erythrocytes. This review highlights some of the recent advances and key knowledge gaps in protein trafficking pathways in P. falciparum-infected red cells and speculates on the impact of exported gene families in the trafficking pathway., Parasitology, 141(12), pp.1533-1543; 2014},
 pages = {1533--1543},
 title = {Protein trafficking in Plasmodium falciparum-infected red cells and impact of the expansion of exported protein families},
 volume = {141},
 year = {2014}
}