Malaria parasites adopt host cell superoxide dismutase

Science ◽  
1983 ◽  
Vol 221 (4612) ◽  
pp. 764-766 ◽  
Author(s):  
A. Fairfield ◽  
Meshnick ◽  
J. Eaton
Keyword(s):  
Superoxide Dismutase ◽  
Host Cell ◽  
Malaria Parasites

scholarly journals Organization of ETRAMPs and EXP-1 at the parasite-host cell interface of malaria parasites

2006 ◽  
Vol 59 (3) ◽  
pp. 779-794 ◽  
Author(s):  
Tobias Spielmann ◽  
Donald L. Gardiner ◽  
Hans-Peter Beck ◽  
Katharine R. Trenholme ◽  
David J. Kemp
Keyword(s):  
Host Cell ◽  
Malaria Parasites ◽  
Cell Interface

Excess haemoglobin digestion by malaria parasites: a strategy to prevent premature host cell lysis

2004 ◽  
Vol 32 (3) ◽  
pp. 353-359 ◽  
Author(s):  
Virgilio L Lew ◽  
Lynn Macdonald ◽  
Hagai Ginsburg ◽  
Miriam Krugliak ◽  
Teresa Tiffert
Keyword(s):  
Host Cell ◽  
Cell Lysis ◽  
Malaria Parasites

Elucidating Host Cell Uptake by Malaria Parasites

2019 ◽  
Vol 35 (5) ◽  
pp. 333-335 ◽  
Author(s):  
Brendan Elsworth ◽  
Caroline D. Keroack ◽  
Manoj T. Duraisingh
Keyword(s):  
Host Cell ◽  
Cell Uptake ◽  
Malaria Parasites

Host cell remodelling in malaria parasites: a new pool of potential drug targets

2017 ◽  
Vol 47 (2-3) ◽  
pp. 119-127 ◽  
Author(s):  
Paul R. Gilson ◽  
Scott A. Chisholm ◽  
Brendan S. Crabb ◽  
Tania F. de Koning-Ward
Keyword(s):  
Host Cell ◽  
Drug Targets ◽  
Potential Drug ◽  
Malaria Parasites ◽  
Potential Drug Targets

scholarly journals Characterization of apicomplexan amino acid transporters (ApiATs) in the malaria parasite Plasmodium falciparum

2021 ◽  
Author(s):  
Jan Stephan Wichers ◽  
Carolina van Gelder ◽  
Gwendolin Fuchs ◽  
Julia Mareike Ruge ◽  
Emma Pietsch ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Host Cell ◽  
Amino Acid Transporters ◽  
Asexual Parasite ◽  
Malaria Parasites ◽  
Functional Inactivation ◽  
Uptake Of Nutrients

ABSTRACTDuring the symptomatic human blood phase, malaria parasites replicate within red blood cells. Parasite proliferation relies on the uptake of nutrients, such as amino acids, from the host cell and the blood plasma, requiring transport across multiple membranes. Amino acids are delivered to the parasite through the parasite surrounding vacuolar compartment by specialized nutrient-permeable channels of the erythrocyte membrane and the parasitophorous vacuole membrane (PVM). However, further transport of amino acid across the parasite plasma membrane (PPM) is currently not well characterized. In this study, we focused on a family of Apicomplexan amino acid transporters (ApiATs) that comprises five members in Plasmodium falciparum. First, we localized four of the PfApiATs at the PPM using endogenous GFP-tagging. Next, we applied reverse genetic approaches to probe into their essentiality during asexual replication and gametocytogenesis. Upon inducible knockdown and targeted gene disruption a reduced asexual parasite proliferation was detected for PfApiAT2 and PfApiAT4. Functional inactivation of individual PfApiATs targeted in this study had no effect on gametocyte development. Our data suggest that individual PfApiATs are partially redundant during asexual in vitro proliferation and fully redundant during gametocytogenesis of P. falciparum parasites.IMPORTANCEMalaria parasites live and multiply inside cells. To facilitate their extremely fast intracellular proliferation they hijack and transform their host cells. This also requires the active uptake of nutrients, such as amino acids, from the host cell and the surrounding environment through various membranes that are the consequence of the parasite’s intracellular lifestyle. In this manuscript we focus on a family of putative amino acid transporters termed ApiAT. We show expression and localization of four transporters in the parasite plasma membrane of Plasmodium falciparum-infected erythrocytes that represent one interface of the pathogen to its host cell. We probed into the impact of functional inactivation of individual transporters on parasite growth in asexual and sexual blood stages of P. falciparum and reveal that only two of them show a modest but significant reduction in parasite proliferation but no impact on gametocytogenesis pointing towards redundancy within this transporter family.

scholarly journals Iron robbery by intracellular pathogen via bacterial effector–induced ferritinophagy

2021 ◽  
Vol 118 (23) ◽  
pp. e2026598118
Author(s):  
Qi Yan ◽  
Wenqing Zhang ◽  
Mingqun Lin ◽  
Omid Teymournejad ◽  
Khemraj Budachetri ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Host Cell ◽  
Host Cells ◽  
Ammonium Citrate ◽  
Ferric Ammonium Citrate ◽  
Type Iv ◽  
Cellular Iron ◽  
Ferric Ammonium ◽  
Iron Pool ◽  
Human Monocytic Ehrlichiosis

Iron is essential for survival and proliferation of Ehrlichia chaffeensis, an obligatory intracellular bacterium that causes an emerging zoonosis, human monocytic ehrlichiosis. However, how Ehrlichia acquires iron in the host cells is poorly understood. Here, we found that native and recombinant (cloned into the Ehrlichia genome) Ehrlichia translocated factor-3 (Etf-3), a previously predicted effector of the Ehrlichia type IV secretion system (T4SS), is secreted into the host cell cytoplasm. Secreted Etf-3 directly bound ferritin light chain with high affinity and induced ferritinophagy by recruiting NCOA4, a cargo receptor that mediates ferritinophagy, a selective form of autophagy, and LC3, an autophagosome biogenesis protein. Etf-3−induced ferritinophagy caused ferritin degradation and significantly increased the labile cellular iron pool, which feeds Ehrlichia. Indeed, an increase in cellular ferritin by ferric ammonium citrate or overexpression of Etf-3 or NCOA4 enhanced Ehrlichia proliferation, whereas knockdown of Etf-3 in Ehrlichia via transfection with a plasmid encoding an Etf-3 antisense peptide nucleic acid inhibited Ehrlichia proliferation. Excessive ferritinophagy induces the generation of toxic reactive oxygen species (ROS), which could presumably kill both Ehrlichia and host cells. However, during Ehrlichia proliferation, we observed concomitant up-regulation of Ehrlichia Fe-superoxide dismutase, which is an integral component of Ehrlichia T4SS operon, and increased mitochondrial Mn-superoxide dismutase by cosecreted T4SS effector Etf-1. Consequently, despite enhanced ferritinophagy, cellular ROS levels were reduced in Ehrlichia-infected cells compared with uninfected cells. Thus, Ehrlichia safely robs host cell iron sequestered in ferritin. Etf-3 is a unique example of a bacterial protein that induces ferritinophagy to facilitate pathogen iron capture.

Host-cell invasion by malaria parasites: insights from Plasmodium and Toxoplasma

2008 ◽  
Vol 24 (12) ◽  
pp. 557-563 ◽  
Author(s):  
Jake Baum ◽  
Tim-Wolf Gilberger ◽  
Freddy Frischknecht ◽  
Markus Meissner
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Host Cell Invasion ◽  
Malaria Parasites

Nanomimics of Host Cell Membranes Block Invasion and Expose Invasive Malaria Parasites

ACS Nano ◽  
2014 ◽  
Vol 8 (12) ◽  
pp. 12560-12571 ◽  
Author(s):  
Adrian Najer ◽  
Dalin Wu ◽  
Andrej Bieri ◽  
Françoise Brand ◽  
Cornelia G. Palivan ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Membranes ◽  
Malaria Parasites ◽  
Host Cell Membranes
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