Author: ["Z.Q. Bonday","S. Dhanasekaran","P.N. Rangarajan","G. Padmanaban"]
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Abstract
The parasite Plasmodium berghei imports the enzyme δ-aminolevulinate dehydratase (ALAD), and perhaps the subsequent enzymes of the pathway from the host red blood cell to sustain heme synthesis. Here we have studied the mechanism of this import. A 65-kDa protein on the P. berghei membrane specifically bound to mouse red blood cell ALAD, and a 93-amino-acid fragment (ALAD-ΔNC) of the host erythrocyte ALAD was able to compete with the full-length enzyme for binding to the P. berghei membrane. ALAD-ΔNC was taken up by the infected red blood cell when added to a culture of P. falciparum and this led to a substantial decrease in ALAD protein and enzyme activity and, subsequently, heme synthesis in the parasite, resulting in its death.Cite this article
Bonday, Z., Dhanasekaran, S., Rangarajan, P. et al. Import of host δ-aminolevulinate dehydratase into the malarial parasite: Identification of a new drug target. Nat Med 6, 898–903 (2000). https://doi.org/10.1038/78659 