Nov 12, 2013

Analyses of interactions between heparin and the apical surface proteins of Plasmodium falciparum

Scientific Reports
Kyousuke KobayashiKentaro Kato

Abstract

Heparin, a sulfated glycoconjugate, reportedly inhibits the blood-stage growth of the malaria parasite Plasmodium falciparum. Elucidation of the inhibitory mechanism is valuable for developing novel invasion-blocking treatments based on heparin. Merozoite surface protein 1 has been reported as a candidate target of heparin; however, to better understand the molecular mechanisms involved, we characterized the molecules that bind to heparin during merozoite invasion. Here, we show that heparin binds only at the apical tip of the merozoite surface and that multiple heparin-binding proteins localize preferentially in the apical organelles. To identify heparin-binding proteins, parasite proteins were fractionated by means of heparin affinity chromatography and subjected to immunoblot analysis with ligand-specific antibodies. All tested members of the Duffy and reticulocyte binding-like families bound to heparin with diverse affinities. These findings suggest that heparin masks the apical surface of merozoites and blocks interaction with the erythrocyte membrane after initial attachment.

Mentioned in this Paper

Merozoites
Heparin
Immunoblotting
Reticulocytes
Malaria
Malaria Vaccines
Binding Protein
Binding (Molecular Function)
Membrane Proteins
Erythrocyte Membrane

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