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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

04/1990

Volume

61

Pages

243 - 254

Addresses

Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115.

Keywords

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