scholarly journals Origins of the parasitophorous vacuole membrane of the malaria parasite, Plasmodium falciparum, in human red blood cells

1992 ◽  
Vol 102 (3) ◽  
pp. 527-532 ◽  
Author(s):  
A.R. Dluzewski ◽  
G.H. Mitchell ◽  
P.R. Fryer ◽  
S. Griffiths ◽  
R.J. Wilson ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Cell Membrane ◽  
Host Cell ◽  
Malaria Parasite ◽  
Parasitophorous Vacuole ◽  
Parasitophorous Vacuole Membrane ◽  
Host Cell Membrane ◽  
Vacuole Membrane ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

We have attempted to determine whether the parasitophorous vacuole membrane, in which the malaria parasite (merozoite) encapsulates itself when it enters a red blood cell, is derived from the host cell plasma membrane, as the appearance of the invasion process in the electron microscope has been taken to suggest, or from lipid material stored in the merozoite. We have incorporated into the red cell membrane a haptenic phospholipid, phosphatidylethanolamine, containing an NBD (N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)) group, substituted in the acyl chain, and allowed it to translocate into the inner bilayer leaflet. After invasion of these labelled cells by the parasite, Plasmodium falciparum, immuno-gold electron microscopy was used to follow the distribution of the labelled lipid; this was found to be overwhelmingly in favour of the host cell membrane relative to the parasitophorous vacuole. Merozoites of P. knowlesi were allowed to attach irreversibly to red cells without invasion, using the method of pretreatment with cytochalasin. The region of contact between the merozoite and the host cell membrane was in all cases devoid of the labelled phosphatidylethanolamine. These results lead us to infer that the parasitophorous vacuole membrane is derived wholly or partly from lipid preexisting in the merozoite.

Transport of the essential nutrient isoleucine in human erythrocytes infected with the malaria parasite Plasmodium falciparum

Blood ◽  
2006 ◽  
Vol 109 (5) ◽  
pp. 2217-2224 ◽  
Author(s):  
Rowena E. Martin ◽  
Kiaran Kirk
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Malaria Parasite ◽  
Human Erythrocytes ◽  
Extracellular Medium ◽  
Host Cell Membrane ◽  
Trophozoite Stage ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Essential Nutrient

AbstractThe intraerythrocytic malaria parasite derives much of its requirement for amino acids from the digestion of the hemoglobin of its host cell. However, one amino acid, isoleucine, is absent from adult human hemoglobin and must therefore be obtained from the extracellular medium. In this study we have characterized the mechanisms involved in the uptake of isoleucine by the intraerythrocytic parasite. Under physiologic conditions the rate of transport of isoleucine into human erythrocytes infected with mature trophozoite-stage Plasmodium falciparum parasites is increased to approximately 5-fold that in uninfected cells, with the increased flux being via the new permeability pathways (NPPs) induced by the parasite in the host cell membrane. Transport via the NPPs ensures that protein synthesis is not rate limited by the flux of isoleucine across the erythrocyte membrane. On entering the infected erythrocyte, isoleucine is taken up into the parasite via a saturable, ATP-, Na+-, and H+-independent system which has the capacity to mediate the influx of isoleucine in exchange for leucine (liberated from hemoglobin). The accumulation of radiolabeled isoleucine within the parasite is mediated by a second (high-affinity, ATP-dependent) mechanism, perhaps involving metabolism and/or the concentration of isoleucine within an intracellular organelle.

scholarly journals A revised mechanism for how Plasmodium falciparum recruits and exports proteins into its erythrocytic host cell.

2021 ◽  
Author(s):  
Mikha Gabriela ◽  
Kathryn Matthews ◽  
Cas Boshoven ◽  
Betty Kouskousis ◽  
David Steer ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Parasitophorous Vacuole ◽  
Specific Interactions ◽  
Parasitophorous Vacuole Membrane ◽  
Conducting Channel ◽  
Trophozoite Stage ◽  
Vacuole Membrane ◽  
N Terminus ◽  
Exported Protein

Plasmodium falciparum exports ~10% of its proteome into its host erythrocyte to modify the host cell’s physiology. The Plasmodium export element (PEXEL) motif contained within the N-terminus of most exported proteins directs the trafficking of those proteins into the erythrocyte. To reach the host cell, the PEXEL motif of exported proteins are processed by the endoplasmic reticulum (ER) resident aspartyl protease plasmepsin V. Then, following secretion into the parasite-encasing parasitophorous vacuole, the mature exported protein must be unfolded and translocated across the parasitophorous vacuole membrane by the Plasmodium translocon of exported proteins (PTEX). PTEX is a protein-conducting channel consisting of the pore-forming protein EXP2, the protein unfoldase HSP101, and structural component PTEX150. The mechanism of how exported proteins are specifically trafficked from the parasite’s ER following PEXEL cleavage to PTEX complexes on the parasitophorous vacuole membrane is currently not understood. Here, we present evidence that EXP2 and PTEX150 form a stable subcomplex that facilitates HSP101 docking. We also demonstrate that HSP101 localises both within the parasitophorous vacuole and within the parasite’s ER throughout the ring and trophozoite stage of the parasite, coinciding with the timeframe of protein export. Interestingly, we found that HSP101 can form specific interactions with model PEXEL proteins in the parasite ER, irrespective of their PEXEL processing status. Collectively, our data suggest that HSP101 recognises and chaperones PEXEL proteins from the ER to the parasitophorous vacuole and given HSP101’s specificity for the EXP2-PTEX150 subcomplex, this provides a mechanism for how exported proteins are specifically targeted to PTEX for translocation into the erythrocyte.

The origin of parasitophorous vacuole membrane lipids in malaria-infected erythrocytes

1993 ◽  
Vol 106 (1) ◽  
pp. 237-248 ◽  
Author(s):  
G.E. Ward ◽  
L.H. Miller ◽  
J.A. Dvorak
Keyword(s):  
Host Cell ◽  
Erythrocyte Membrane ◽  
Membrane Lipids ◽  
Parasitophorous Vacuole ◽  
Light Level ◽  
Surface Proteins ◽  
Parasitophorous Vacuole Membrane ◽  
Host Cell Membrane ◽  
Vacuole Membrane ◽  
Erythrocyte Surface

During invasion of an erythrocyte by a malaria merozoite, an indentation develops in the erythrocyte surface at the point of contact between the two cells. This indentation deepens as invasion progresses, until the merozoite is completely surrounded by a membrane known as the parasitophorous vacuole membrane (PVM). We incorporated fluorescent lipophilic probes and phospholipid analogs into the erythrocyte membrane, and followed the fate of these probes during PVM formation with low-light-level video fluorescence microscopy. The concentration of probe in the forming PVM was indistinguishable from the concentration of probe in the erythrocyte membrane, suggesting that the lipids of the PVM are continuous with and derived from the host cell membrane during invasion. In contrast, fluorescently labeled erythrocyte surface proteins were largely excluded from the forming PVM. These data are consistent with a model for PVM formation in which the merozoite induces a localized invagination in the erythrocyte lipid bilayer, concomitant with a localized restructuring of the host cell cytoskeleton.

scholarly journals Spatial Organization of the Blood Stage Parasitophorous Vacuole of the Malaria Parasite Plasmodium falciparum

2019 ◽  
Vol 116 (3) ◽  
pp. 456a
Author(s):  
Matthias Garten ◽  
Josh R. Beck ◽  
Robyn Roth ◽  
Christopher K.E. Bleck ◽  
John E. Heuser ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Spatial Organization ◽  
Parasitophorous Vacuole ◽  
Blood Stage ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

scholarly journals Host cell deformability is linked to transmission in the human malaria parasite Plasmodium falciparum

2012 ◽  
Vol 14 (7) ◽  
pp. 983-993 ◽  
Author(s):  
Mythili Aingaran ◽  
Rou Zhang ◽  
Sue KaYee Law ◽  
Zhangli Peng ◽  
Andreas Undisz ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Malaria Parasite ◽  
Cell Deformability ◽  
Human Malaria Parasite ◽  
Human Malaria ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

scholarly journals Selective permeabilization of the host cell membrane of Plasmodium falciparum-infected red blood cells with streptolysin O and equinatoxin II

2007 ◽  
Vol 403 (1) ◽  
pp. 167-175 ◽  
Author(s):  
Katherine E. Jackson ◽  
Tobias Spielmann ◽  
Eric Hanssen ◽  
Akinola Adisa ◽  
Frances Separovic ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Cell Membrane ◽  
Red Blood Cells ◽  
Host Cell ◽  
Blood Cells ◽  
Parasitophorous Vacuole ◽  
Host Cell Membrane ◽  
Streptolysin O ◽  
Infected Rbcs ◽  
Equinatoxin Ii

Plasmodium falciparum develops within the mature RBCs (red blood cells) of its human host in a PV (parasitophorous vacuole) that separates the host cell cytoplasm from the parasite surface. The pore-forming toxin, SLO (streptolysin O), binds to cholesterol-containing membranes and can be used to selectively permeabilize the host cell membrane while leaving the PV membrane intact. We found that in mixtures of infected and uninfected RBCs, SLO preferentially lyses uninfected RBCs rather than infected RBCs, presumably because of differences in cholesterol content of the limiting membrane. This provides a means of generating pure preparations of viable ring stage infected RBCs. As an alternative permeabilizing agent we have characterized EqtII (equinatoxin II), a eukaryotic pore-forming toxin that binds preferentially to sphingomyelin-containing membranes. EqtII lyses the limiting membrane of infected and uninfected RBCs with similar efficiency but does not disrupt the PV membrane. It generates pores of up to 100 nm, which allow entry of antibodies for immunofluorescence and immunogold labelling. The present study provides novel tools for the analysis of this important human pathogen and highlights differences between Plasmodium-infected and uninfected RBCs.

Sign in / Sign up

Export Citation Format

Share Document