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@ARTICLE{Wunderlich:635879,
author = {Wunderlich, Juliane and Kotov, Vadim and Votborg-Novél,
Lasse and Ntalla, Christina and Geffken, Maria and Peine,
Sven and Portugal, Silvia and Strauss, Jan},
title = {{I}ron transport pathways in the human malaria parasite
{P}lasmodium falciparum revealed by {RNA}-sequencing},
journal = {Frontiers in Cellular and Infection Microbiology},
volume = {14},
issn = {2235-2988},
address = {Lausanne},
publisher = {Frontiers Media},
reportid = {PUBDB-2025-03563},
pages = {1480076},
year = {2024},
abstract = {Host iron deficiency is protective against severe malaria
as the human malaria parasite Plasmodium falciparum depends
on bioavailable iron from its host to proliferate. The
essential pathways of iron acquisition, storage, export, and
detoxification in the parasite differ from those in humans,
as orthologs of the mammalian transferrin receptor,
ferritin, or ferroportin, and a functional heme oxygenase
are absent in P. falciparum. Thus, the proteins involved in
these processes may be excellent targets for therapeutic
development, yet remain largely unknown. Here, we show that
parasites cultured in erythrocytes from an iron-deficient
donor displayed significantly reduced growth rates compared
to those grown in red blood cells from healthy controls.
Sequencing of parasite RNA revealed diminished expression of
genes involved in overall metabolism, hemoglobin digestion,
and metabolite transport under low-iron versus control
conditions. Supplementation with hepcidin, a specific
ferroportin inhibitor, resulted in increased labile iron
levels in erythrocytes, enhanced parasite replication, and
transcriptional upregulation of genes responsible for
merozoite motility and host cell invasion. Through
endogenous GFP tagging of differentially expressed putative
transporter genes followed by confocal live-cell imaging,
proliferation assays with knockout and knockdown lines, and
protein structure predictions, we identified six proteins
that are likely required for ferrous iron transport in P.
falciparum. Of these, we localized PfVIT and PfZIPCO to
cytoplasmic vesicles, PfMRS3 to the mitochondrion, and the
novel putative iron transporter PfE140 to the plasma
membrane for the first time in P. falciparum. PfNRAMP/PfDMT1
and PfCRT were previously reported to efflux Fe$^{2+}$ from
the digestive vacuole. Our data support a new model for
parasite iron homeostasis, in which PfE140 is involved in
iron uptake across the plasma membrane, PfMRS3 ensures
non-redundant Fe$^{2+}$ supply to the mitochondrion as the
main site of iron utilization, PfVIT transports excess iron
into cytoplasmic vesicles, and PfZIPCO exports Fe$^{2+}$
from these organelles in case of iron scarcity. These
results provide new insights into the parasite’s response
to differential iron availability in its environment and
into the mechanisms of iron transport in P. falciparum as
promising candidate targets for future antimalarial drugs.},
cin = {CSSB-EMBL-CL},
ddc = {610},
cid = {I:(DE-H253)CSSB-EMBL-CL-20210806},
pnm = {899 - ohne Topic (POF4-899) / DrySeasonPf - Dry season P.
falciparum reservoir (759534)},
pid = {G:(DE-HGF)POF4-899 / G:(EU-Grant)759534},
experiment = {EXP:(DE-H253)ALFM-20250101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:39575308},
doi = {10.3389/fcimb.2024.1480076},
url = {https://bib-pubdb1.desy.de/record/635879},
}