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. 2016 Jan 29;15:51. doi: 10.1186/s12936-016-1097-9

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© Ponsuwanna et al. 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — Diagram depicting haemoglobin degradation and haemozoin synthesis in Plasmodium falciparum. Haemoglobin is taken up into the parasite via cytostome, passing through parasite membrane and parasitophorous vacuole membrane (PVM). Double-membrane vesicle containing red blood cell content as observed in a cross-section delivers Hb into the food vacuole [50]. A series of proteases in the plasmepsin (PM), falcipain (FP) and falcilysin (FLN) family digest Hb into either free amino acid or short peptide. Haem from digested Hb is packed into polymerized crystal called haemozoin with help from haem detoxification protein (HDP) and histidine-rich protein (HRP). Lipid biomolecules from either food vacuole membrane or droplet are suggested to promote haemozoin synthesis probably by seeding and directing crystal growth [51]