Abstract
Several observations suggest that iron is essential for the development of malaria parasites1–6 but there is evidence that the parasites in erythrocytes do not obtain iron from haemoglobin. The total haemin level in parasitized erythrocytes does not vary during parasite development7, indicating that the iron-containing moiety of haemoglobin is not detectably metabolized. Although parasite proteases can degrade the protein part of haemoglobin in red cells8,9, no parasite enzymes that degrade haemin have been identified. In mammalian cells, haemin is degraded to carbon monoxide and bilirubin by the enzyme haeme oxygenase10. This enzyme has not been found in malaria parasites11. In fact haemin has been found to be toxic to parasite carbohydrate metabolism12. Thus, iron apparently cannot be liberated from haemin and instead is sequestered in infected red cells as haemozoin, the characteristic pigment associated with malarial infection13,14. If iron bound to transferrin is the source of ferric ions for malaria parasites within mature erythrocytes, then the parasite must synthesize its own transferrin receptor and localize it on the surface of the infected cell, because the receptors for transferrin are lost during erythrocyte maturation5,16. Our results here suggest that Plasmodium falciparum synthesizes its own transferrin receptors enabling it to take up iron from transferrin by receptor-mediated endocytosis.
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Rodriguez, M., Jungery, M. A protein on Plasmodium falciparum-infected erythrocytes functions as a transferrin receptor. Nature 324, 388–391 (1986). https://doi.org/10.1038/324388a0
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DOI: https://doi.org/10.1038/324388a0
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