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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.

Original publication




Journal article



Publication Date





71 - 81


Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, Binding Sites, Cell Adhesion, Cell Adhesion Molecules, Epitopes, Erythrocytes, Humans, Intercellular Adhesion Molecule-1, Lymphocyte Function-Associated Antigen-1, Malaria, Falciparum, Mice, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Oligodeoxyribonucleotides, Plasmodium falciparum, Protein Conformation, Receptors, Virus, Sequence Homology, Nucleic Acid