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Intercellular adhesion molecule 1 (ICAM-1, CD54) binds to the integrin LFA-1 (CD11a/CD18), promoting cell adhesion in immune and inflammatory reactions. ICAM-1 is also subverted as a receptor by the major group of rhinoviruses. Electron micrographs show that ICAM-1 is a bent rod, 18.7 nm long, suggesting a model in which the five immunoglobulin-like domains are oriented head to tail at a small angle to the rod axis. ICAM-1 sequences important to binding LFA-1, rhinovirus, and four monoclonal antibodies were identified through the characterization of chimeric ICAM-1 molecules and mutants. The amino-terminal two immunoglobulin-like domains of ICAM-1 appear to interact conformationally. Domain 1 of ICAM-1 contains the primary site of contact for both LFA-1 and rhinovirus; the presence of domains 3-5 markedly affects the accessibility of the binding site for rhinovirus and less so for LFA-1. The binding sites appear to be distinct but overlapping; rhinovirus binding also differs from LFA-1 binding in its lack of divalent cation dependence. Our analysis suggests that rhinoviruses mimic LFA-1 in binding to the most membrane-distal, and thus most accessible, site of ICAM-1.

Original publication

DOI

10.1016/0092-8674(90)90805-o

Type

Journal article

Journal

Cell

Publication Date

20/04/1990

Volume

61

Pages

243 - 254

Keywords

Amino Acid Sequence, Animals, Antigens, CD, Antigens, Differentiation, Cell Adhesion Molecules, Cell Line, Chimera, Chromosome Deletion, Humans, Immunoglobulins, Intercellular Adhesion Molecule-1, Kinetics, Lymphocyte Function-Associated Antigen-1, Membrane Glycoproteins, Mice, Models, Molecular, Molecular Sequence Data, Mutation, Oligonucleotide Probes, Protein Binding, Protein Conformation, Receptors, Leukocyte-Adhesion, Receptors, Virus, Rhinovirus