Analyses of Interactions Between Heparin and the Apical Surface Proteins of Plasmodium falciparum
| Autor: | Hitoshi Takemae, Hiroomi Akashi, Kyousuke Kobayashi, Akiko Ishiwa, Taisuke Horimoto, Haiyan Gong, Tatsuki Sugi, Frances C. Recuenco, Kentaro Kato, Tatsuya Iwanaga, Ryo Takano |
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| Rok vydání: | 2013 |
| Předmět: |
Erythrocytes
Glycoconjugate Plasmodium falciparum Protozoan Proteins Antigens Protozoan Article Sulfation Reticulocyte Affinity chromatography Organelle medicine Humans Merozoite Surface Protein 1 chemistry.chemical_classification Multidisciplinary biology Heparin Membrane Proteins Receptor Protein-Tyrosine Kinases biology.organism_classification medicine.anatomical_structure Biochemistry chemistry Immunology biology.protein Antibody Protein Binding medicine.drug |
| Zdroj: | Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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