Abstract
Phospholipid membranes are thought to be one of the main inducers of hemozoin formation in Plasmodia and other blood-feeding parasites. The “membrane surrounding hemozoin” has been observed in infected cells but has not been observed in in vitro experiments. This study focused on observing the association of phospholipid membranes and synthetic β-hematin, which is chemically identical to hemozoin, and on a further exploration into the mechanism of phospholipid membrane-induced β-hematin formation. Our results showed that β-hematin formation was induced by phospholipids in the fluid phase but not in the gel phase. The ability of phospholipids to induce β-hematin formation was inversely correlated with gel-to-liquid phase transition temperatures, suggesting an essential insertion of heme into the hydrocarbon chains of the phospholipid membrane to form β-hematin. For this study, a cryogenic transmission electron microscope was used to achieve the first direct observation of the formation of a monolayer of phospholipid membrane surrounding β-hematin.
Highlights
Malaria is one of the most common diseases in tropical countries
Hemozoin is known to be structurally and chemically identical to in vitro synthetic bhematin (BH), which is a crystal of the heme (Fe(III)PPIX) dimer of the hematin Fe (III) PPIX dimer [15,16,17]
It is suggested that the blocking of BH formation is an ideal target for antimalarial screening [23,24,25,26]; it is important to understand the mechanism of BH formation
Summary
Malaria is one of the most common diseases in tropical countries. Each year, there are an estimated 225 million new malaria infections and almost a million deaths due to malaria world-wide [1]. Host protein digestion has two aspects: to obtain amino acids and to regulate osmotic pressure This hemoglobin digestion takes place in the parasites’ food vacuoles and is carried out by multiple proteases including four aspartic versions [3]: three cysteine proteases [4] and a zinc metalloprotease (falsilysin) [5]. Hemozoin is known to be structurally and chemically identical to in vitro synthetic bhematin (BH), which is a crystal of the heme (Fe(III)PPIX) dimer of the hematin Fe (III) PPIX dimer [15,16,17] It has been used for parasite concentration and detection [18,19,20,21,22]. It is suggested that the blocking of BH formation is an ideal target for antimalarial screening [23,24,25,26]; it is important to understand the mechanism of BH formation
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