scholarly journals The Malaria Parasite Supplies Glutathione to its Host Cell - Investigation of Glutathione Transport and Metabolism in Human Erythrocytes Infected with Plasmodium Falciparum

1997 ◽  
Vol 250 (3) ◽  
pp. 670-679 ◽  
Author(s):  
Hani Atamna ◽  
Hagai Ginsburg
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Malaria Parasite ◽  
Human Erythrocytes ◽  
Glutathione Transport

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 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.

scholarly journals Signal-mediated export of proteins from the malaria parasite to the host erythrocyte

2005 ◽  
Vol 171 (4) ◽  
pp. 587-592 ◽  
Author(s):  
Matthias Marti ◽  
Jake Baum ◽  
Melanie Rug ◽  
Leann Tilley ◽  
Alan F. Cowman
Keyword(s):  
Host Cell ◽  
Malaria Parasite ◽  
Human Erythrocytes ◽  
Virulence Proteins ◽  
Genus Plasmodium ◽  
Intracellular Parasites

Intracellular parasites from the genus Plasmodium reside and multiply in a variety of cells during their development. After invasion of human erythrocytes, asexual stages from the most virulent malaria parasite, P. falciparum, drastically change their host cell and export remodelling and virulence proteins. Recent data demonstrate that a specific NH2-terminal signal conserved across the genus Plasmodium plays a central role in this export process.

scholarly journals Protein trafficking in Plasmodium falciparum-infected red cells and impact of the expansion of exported protein families

Parasitology ◽  
2014 ◽  
Vol 141 (12) ◽  
pp. 1533-1543 ◽  
Author(s):  
SURENDRA K. PRAJAPATI ◽  
RICHARD CULLETON ◽  
OM P. SINGH
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Protein Trafficking ◽  
Malaria Parasite ◽  
Functional Characterization ◽  
Gene Families ◽  
Red Cells ◽  
Protein Families ◽  
The Impact ◽  
Export Signal

SUMMARYErythrocytes 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.

Water and urea transport in human erythrocytes infected with the malaria parasite Plasmodium falciparum

1990 ◽  
Vol 40 (2) ◽  
pp. 269-278 ◽  
Author(s):  
Mary Ann Zanner ◽  
William R. Galey ◽  
Joseph V. Scaletti ◽  
Jesper Brahm ◽  
David L. Vander Jagt
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Human Erythrocytes ◽  
Urea Transport ◽  
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 Enhanced choline and Rb+ transport in human erythrocytes infected with the malaria parasite Plasmodium falciparum

1991 ◽  
Vol 278 (2) ◽  
pp. 521-525 ◽  
Author(s):  
K Kirk ◽  
H Y Wong ◽  
B C Elford ◽  
C I Newbold ◽  
J C Ellory
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Human Erythrocytes ◽  
Transport Pathway ◽  
Choline Transport ◽  
Transport Component ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Infected Cells

Human erythrocytes infected in vitro with the malaria parasite Plasmodium falciparum showed a markedly increased rate of choline influx compared with normal cells. Choline transport into uninfected cells (cultured in parallel with infected cells) obeyed Michaelis-Menten kinetics (Km approximately 11 microM). In malaria-parasite-infected cells there was an additional choline-transport component which failed to saturate at extracellular concentrations of up to 500 microM. This component was less sensitive than the endogenous transporter to inhibition by the Cinchona bark alkaloids quinine, quinidine, cinchonine and cinchonidine, but showed a much greater sensitivity than the native system to inhibition by piperine. The sensitivity of the induced choline transport to these reagents was similar to that of the malaria-induced (ouabain- and bumetanide-resistant) Rb(+)-transport pathway; however, the relative magnitudes of the piperine-sensitive choline and Rb+ fluxes in malaria-parasite-infected cells varied between cultures. This suggests either that the enhanced transport of the two cations was via functionally distinct (albeit pharmacologically similar) pathways, or that the transport was mediated by a pathway with variable substrate selectivity.

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