As a result, during infection there is a constant battle between the host and the invader for iron, in which the invader tries to get access to host iron, and the host arranges complex iron-withholding mechanisms to prevent it. Iron-seeking parasites use all iron-containing proteins in eukaryotes as iron sources; they have developed several elaborate strategies to do so. The parasites’ ability to capture and absorb iron from the host is considered a determinant of their virulence.
An article by G. Ortiz-Estrada et al. discusses possible ways in which the human enteric parasite Entamoeba histolytica might obtain access to bovine lactoferrin, a protein found in milk mainly consumed by babies and infants. In their research article “Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica,” the authors compare virulent trophozoites isolated recently from hamster liver abscesses with nonvirulent trophozoites maintained in in vitro cultures for over 30 years, regarding their interaction with bovine iron. Charged Lf (B-holo-Lf). Even though both amoeba variants use B-holo-Lf as an iron source and endocytose this glycoprotein through clathrin-coated vesicles, their acquisition of iron, binding parameters, and number of protein-binding sites differ. Furthermore, virulent amoebae also endocytose B-holo-Lf via a cholesterol-dependent mechanism; therefore, virulent amoebas endocytose B-holo-Lf more efficiently.
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