title: Review: rhinoviruses and their ICAM receptors.
abstract: The normal function of human intercellular adhesion molecule-1 (ICAM-1) is to provide adhesion between endothelial cells and leukocytes after injury or stress. ICAM-1 binds to leukocyte function-associated antigen or macrophage-1 antigen. However, ICAM-1 is also used as a receptor by the major group of human rhinoviruses and is a catalyst for the subsequent viral uncoating during cell entry. The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2 A resolution and fitted into a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex. Rhinovirus attachment is confined to the BC, CD, DE, and FG loops of the amino-terminal Ig-like domain (D1) at the end distal to the cellular membrane. The loops are considerably different in structure to those of human ICAM-2 or murine ICAM-1, which do not bind rhinoviruses. There are extensive charge interactions between ICAM-1 and human rhinoviruses, which are mostly conserved in both major and minor receptor groups of rhinoviruses.
authors.affiliation: Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA.
authors.forename: J
authors.initials: J
authors.lastname: Bella
authors.forename: M G
authors.initials: MG
authors.lastname: Rossmann
mesh_terms: D000818:Animals; D020285:Cryoelectron Microscopy; D006031:Glycosylation; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000737:chemistry* / Q000648:ultrastructure; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D010963:Plasmodium falciparum / Q000378:metabolism; D017433:Protein Structure, Secondary; D012229:Rhinovirus / Q000737:chemistry* / Q000648:ultrastructure; D014764:Viral Proteins / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D010446:Peptide Fragments; D014764:Viral Proteins; D018799:Intercellular Adhesion Molecule-1