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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 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 evolved to hijack GPC on human erythrocytes during divergence from its ape ancestor.

parasites and vectors

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