Abstract
The intercellular adhesion molecule-1 (ICAM-1, CD54) is one of three putative endothelial receptors that mediate in vitro cytoadherence of P. falciparum-infected erythrocytes. Since cytoadherence to postcapillary venular endothelium is thought to be a major factor in the virulence of P. falciparum malaria, we have examined the interaction between ICAM-1 and the P. falciparum-infected cell, and have compared it with the interaction to the physiological counter receptor, the leukocyte integrin LFA-1. Our results demonstrate that the malaria-binding site resides in the first two domains of the ICAM-1 molecule and overlaps, but is distinct from, the LFA-1 site.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal
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Base Sequence
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Binding Sites
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / immunology
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Cell Adhesion Molecules / physiology*
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Cell Adhesion*
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Epitopes / analysis
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Erythrocytes / parasitology
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Erythrocytes / physiology*
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Humans
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Intercellular Adhesion Molecule-1
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Lymphocyte Function-Associated Antigen-1 / physiology*
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Malaria, Falciparum / blood*
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Mice
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oligodeoxyribonucleotides
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Plasmodium falciparum / physiology*
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Protein Conformation
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Receptors, Virus / physiology*
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Sequence Homology, Nucleic Acid
Substances
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Antibodies, Monoclonal
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Cell Adhesion Molecules
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Epitopes
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Lymphocyte Function-Associated Antigen-1
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Oligodeoxyribonucleotides
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Receptors, Virus
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Intercellular Adhesion Molecule-1