Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites

Blood ◽  
2003 ◽  
Vol 102 (9) ◽  
pp. 3420-3426 ◽  
Author(s):  
Theodore F. Taraschi ◽  
Megan O'Donnell ◽  
Sandra Martinez ◽  
Timothy Schneider ◽  
Darin Trelka ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
G Proteins ◽  
Intracellular Transport ◽  
Surface Membrane ◽  
Plasmodium Falciparum Malaria ◽  
Vesicle Transport ◽  
Aluminum Fluoride ◽  
Sensitive Factor ◽  
Erythrocyte Plasma Membrane

AbstractThe asexual maturation of Plasmodium falciparum is accompanied by the transport of parasite-encoded proteins to the erythrocyte plasma membrane. Activation of G proteins by treatment with aluminum fluoride produced an accumulation within the erythrocyte cytosol of vesicles coated with Plasmodium homologues of COPII and N-ethylmaleimide-sensitive factor, proteins involved in intracellular transport between the Golgi apparatus and the endoplasmic reticulum. These vesicles contain malarial proteins that appear on the erythrocyte plasma membrane, as well as actin and myosin. It is proposed that the parasite adapted a process well established for intracellular transport to mediate the extracellular movement of its proteins through the erythrocyte cytosol to the surface membrane.

scholarly journals Glycosphingolipid GM3 is localized in both exoplasmic and cytoplasmic leaflets of Plasmodium falciparum malaria parasite plasma membrane

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Shiomi Koudatsu ◽  
Tatsunori Masatani ◽  
Rikako Konishi ◽  
Masahito Asada ◽  
Hassan Hakimi ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Malaria Parasite ◽  
Protein Transport ◽  
Vaccine Development ◽  
Parasitophorous Vacuole ◽  
Biological Membrane ◽  
Freeze Fracture ◽  
Plasmodium Falciparum Malaria ◽  
Quick Freezing

AbstractLipid rafts, sterol-rich and sphingolipid-rich microdomains on the plasma membrane are important in processes like cell signaling, adhesion, and protein and lipid transport. The virulence of many eukaryotic parasites is related to raft microdomains on the cell membrane. In the malaria parasite Plasmodium falciparum, glycosylphosphatidylinositol-anchored proteins, which are important for invasion and are possible targets for vaccine development, are localized in the raft. However, rafts are poorly understood. We used quick-freezing and freeze-fracture immuno-electron microscopy to examine the localization of monosialotetrahexosylganglioside (GM1) and monosialodihexosylganglioside (GM3), putative raft microdomain components in P. falciparum and infected erythrocytes. This method immobilizes molecules in situ, minimizing artifacts. GM3 was localized in the exoplasmic (EF) and cytoplasmic leaflets (PF) of the parasite and the parasitophorous vacuole (PV) membranes, but solely in the EF of the infected erythrocyte membrane, as in the case for uninfected erythrocytes. Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) was localized solely in the PF of erythrocyte, parasite, and PV membranes. This is the first time that GM3, the major component of raft microdomains, was found in the PF of a biological membrane. The unique localization of raft microdomains may be due to P. falciparum lipid metabolism and its unique biological processes, like protein transport from the parasite to infected erythrocytes.

Changes Occur in Plasma Membrane Turnover when K562 Leukemia Cells are Induced to Differentiate

1982 ◽  
Vol 40 ◽  
pp. 286-287
Author(s):  
L. M. Marshall
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Intracellular Transport ◽  
Parent Cell ◽  
Membrane Turnover ◽  
Coated Pits ◽  
Surface Distribution ◽  
Specific Proteins ◽  
Erythroleukemic Cell ◽  
Specific Membrane

A human erythroleukemic cell line, metabolically blocked in a late stage of erythropoiesis, becomes capable of differentiation along the normal pathway when grown in the presence of hemin. This process is characterized by hemoglobin synthesis followed by rearrangement of the plasma membrane proteins and culminates in asymmetrical cytokinesis in the absence of nuclear division. A reticulocyte-like cell buds from the nucleus-containing parent cell after erythrocyte specific membrane proteins have been sequestered into its membrane. In this process the parent cell faces two obstacles. First, to organize its erythrocyte specific proteins at one pole of the cell for inclusion in the reticulocyte; second, to reduce or abolish membrane protein turnover since hemoglobin is virtually the only protein being synthesized at this stage. A means of achieving redistribution and cessation of turnover could involve movement of membrane proteins by a directional lipid flow. Generation of a lipid flow towards one pole and accumulation of erythrocyte-specific membrane proteins could be achieved by clathrin coated pits which are implicated in membrane endocytosis, intracellular transport and turnover. In non-differentiating cells, membrane proteins are turned over and are random in surface distribution. If, however, the erythrocyte specific proteins in differentiating cells were excluded from endocytosing coated pits, not only would their turnover cease, but they would also tend to drift towards and collect at the site of endocytosis. This hypothesis requires that different protein species are endocytosed by the coated vesicles in non-differentiating than by differentiating cells.

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