Plasmodium reichenowi EBA-140 merozoite ligand binds to glycophorin D on chimpanzee red blood cells, shedding new light on origins of Plasmodium falciparum

Plasmodium reichenowi EBA-140 merozoite ligand binds to glycophorin D on chimpanzee red blood cells, shedding new light on origins of Plasmodium falciparum

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Abstract Background All symptoms of malaria are caused by the intraerythrocytic proliferation of Plasmodium merozoites.Merozoites invade erythrocytes using multiple binding ligands that recognise specific surface receptors.It has been suggested that adaptation of Plasmodium parasites to infect specific hosts is driven by changes in genes encoding Plasmodium erythrocyte-binding ligands (EBL) and reticulocyte-binding ligands (RBL).

Homologs of both icon track bar f250 EBL and RBL, including the EBA-140 merozoite ligand, have been identified in P.falciparum and P.reichenowi, which infect humans and chimpanzees, respectively.

The P.falciparum EBA-140 was shown to bind human glycophorin C, a minor erythrocyte sialoglycoprotein.Until now, the erythrocyte receptor for the P.

reichenowi EBA-140 remained unknown.Methods The baculovirus expression vector system was used to obtain the recombinant EBA-140 Region II, and flow cytometry and immunoblotting methods were applied to characterise its specificity.Results We showed that the chimpanzee glycophorin D is the receptor for the P.

reichenowi EBA-140 ligand on chimpanzee red blood cells.Conclusions We propose that the development of glycophorin C specificity is spurred by the P.falciparum lineage.

We speculate that the P.falciparum EBA-140 weleda skin food 75ml best price evolved to hijack GPC on human erythrocytes during divergence from its ape ancestor.