ArticleMalaria journal2021
Characterization of the substrate binding site of an iron detoxifying membrane transporter from Plasmodium falciparum.
Article in Malaria journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Infected erythrocytes and plasma proteomics reveal a specific protein signature of severe malaria.EMBO molecular medicine · 2024Article
- Iron transport pathways in the human malaria parasiteFrontiers in cellular and infection microbiology · 2024Article
- The vacuolar iron transporter mediates iron detoxification in Toxoplasma gondii.Nature communications · 2023Article
- Expression and mutagenesis studies in theFrontiers in plant science · 2023Article
- Iron Deprivation Modulates the Exoproteome inFrontiers in cellular and infection microbiology · 2022Article
- Orchestrating a heist: uptake and storage of metals by apicomplexan parasites.Microbiology (Reading, England) · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPlasmodium species are entirely dependent upon their host as a source of essential iron. Although it is an indispensable micronutrient, oxidation of excess ferrous iron to the ferric state in the cell cytoplasm can produce reactive oxygen species that are cytotoxic. The malaria parasite must therefore carefully regulate the processes involved in iron acquisition and storage. A 273 amino acid membrane transporter that is a member of the vacuolar iron transporter (VIT) family and an orthologue of the yeast Ca
methodsUsing the crystal structure of a recently published plant VIT as a template, a high-quality homology model of PfVIT was constructed to identify the amino acid composition of the transporter's substrate binding site and to act as a guide for subsequent mutagenesis studies. To test the effect of mutation of the substrate binding-site residues on PfVIT function a yeast complementation assay assessed the ability of overexpressed, recombinant wild type and mutant PfVIT to rescue an iron-sensitive deletion strain (ccc1∆) of Saccharomyces cerevisiae yeast from the toxic effects of a high concentration of extracellular iron.
resultsThe combined in silico and mutagenesis approach identified a methionine residue located within the cytoplasmic metal binding domain of the transporter as essential for PfVIT function and provided insight into the structural basis for the Fe
conclusionThe structural model of the metal binding site of PfVIT opens the door for rational design of therapeutics to interfere with iron homeostasis within the malaria parasite.
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