Abstract
Micronemal proteins (MICs) are key mediators of cytoadherence and invasion for Toxoplasma gondii. Emerging evidence indicates that carbohydrate binding facilitates Toxoplasma entry into host cells. The recently solved Toxoplasma MIC1s (TgMIC1s) structure reveals the presence of novel specialized domains that can discriminate between glycan residues. Comparison with Plasmodium erythrocyte-binding antigen 175 reveals that terminal sialic acid residues might represent a shared but tailored invasion pathway among apicomplexan parasites.
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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Cell Adhesion
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Cell Adhesion Molecules* / chemistry
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Cell Adhesion Molecules* / genetics
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Cell Adhesion Molecules* / metabolism
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Crystallography, X-Ray
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Host-Parasite Interactions
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Humans
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Ligands
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Models, Molecular
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N-Acetylneuraminic Acid / metabolism
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Protozoan Proteins* / chemistry
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Protozoan Proteins* / genetics
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Protozoan Proteins* / metabolism
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Toxoplasma / pathogenicity*
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Toxoplasma / physiology
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Virulence
Substances
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Cell Adhesion Molecules
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Ligands
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MIC1 protein, Toxoplasma gondii
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Protozoan Proteins
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N-Acetylneuraminic Acid