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- W2766181748 abstract "Plasmodium falciparum, the most lethal malaria parasite species for humans, vastly remodels the mature erythrocyte host cell upon invasion for its own survival. Maurer’s clefts (MC) are membraneous structures established by the parasite in the cytoplasm of infected cells. These organelles are deemed essential for trafficking of virulence complex proteins. The display of the major virulence protein, P. falciparum erythrocyte membrane protein 1 (PfEMP1) on the surface of the infected red blood cell and the subsequent cytoadhesion of infected cells in the microvasculature of vital organs is the key mechanism that leads to the pathology associated with malaria infection. In a previous study we established that PFE60 (PIESP2) is one of the protein components of this complex. Here we demonstrate that PFE60 plays a role in MC lamella segmentation since in the absence of the protein, infected cells display a higher number of stacked MC compared with wild type infected red blood cells. Also, another exported parasite protein (Pf332) failed to localise correctly to the MC in cells lacking PFE60. Furthermore – unlike all other described resident MC membrane proteins – PFE60 does not require its transmembrane regions to be targeted to the organelle. We also provide further evidence that PFE60 is not a red blood cell surface antigen." @default.
- W2766181748 created "2017-11-10" @default.
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- W2766181748 date "2018-01-01" @default.
- W2766181748 modified "2023-10-12" @default.
- W2766181748 title "Plasmodium falciparum exported protein PFE60 influences Maurer’s clefts architecture and virulence complex composition" @default.
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- W2766181748 doi "https://doi.org/10.1016/j.ijpara.2017.09.003" @default.
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