Abstract
Erythrocyte-binding antigen 175 (EBA175) is one of the best-characterized Plasmodium falciparum merozoite ligands; the recently solved crystal structure of EBA175 reveals that terminal sialic acids on the erythrocyte glycoprotein glycophorin A are a crucial factor for erythrocyte recognition by EBA175 because they lock into pockets on its surface. Comparison with Plasmodium reichenowi EBA175 indicates that these interactions have a pivotal role in the host-specific adaptations of parasite ligands.
Publication types
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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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Antigens, Protozoan / physiology*
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Biological Evolution
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Erythrocytes / metabolism
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Erythrocytes / parasitology*
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Glycophorins / metabolism
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Host-Parasite Interactions
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Humans
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Ligands
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Plasmodium falciparum / chemistry*
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Plasmodium falciparum / pathogenicity*
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Plasmodium falciparum / physiology
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Polysaccharides / metabolism
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Protozoan Proteins / chemistry*
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Protozoan Proteins / physiology*
Substances
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Antigens, Protozoan
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Glycophorins
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Ligands
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Polysaccharides
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Protozoan Proteins
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erythrocyte-binding antigen 175, Plasmodium