Abstract
Plasmodium vivax invasion of human erythrocytes requires that the ligand domain of the Duffy-binding protein (DBP) recognize its cognate erythrocyte receptor, making DBP a potential target for therapy. The recently determined crystal structure of the orthologous DBP ligand domain of the closely related simian malaria parasite Plasmodium knowlesi provides insight into the molecular basis for receptor recognition and raises important questions about the mechanism of immune evasion employed by the malaria parasite.
Publication types
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Comment
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, Protozoan / chemistry*
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Binding Sites
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Crystallography, X-Ray
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Humans
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Ligands
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Models, Molecular
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Plasmodium knowlesi / chemistry*
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Plasmodium knowlesi / metabolism
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Plasmodium knowlesi / pathogenicity
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Protein Structure, Tertiary
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Protozoan Proteins / chemistry*
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Receptors, Cell Surface / chemistry*
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Receptors, Cell Surface / metabolism
Substances
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Antigens, Protozoan
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Duffy antigen binding protein, Plasmodium
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Ligands
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Protozoan Proteins
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Receptors, Cell Surface