Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

Cell

Publication Date

10/01/1992

Volume

68

Pages

71 - 81

Keywords

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