Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor

• Published in: The EMBO journal Vol. 18; no. 22; pp. 6249 - 6259
• Main Authors: Kolatkar, Prasanna R., Bella, Jordi, Olson, Norman H., Bator, Carol M., Baker, Timothy S., Rossmann, Michael G.
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 15.11.1999; Blackwell Publishing Ltd
• Subjects: Binding Sites; Canyons; Computer Graphics; cryo-EM; Cryoelectron Microscopy; crystallography; Crystallography, X-Ray; Humans; ICAM-1; Intercellular Adhesion Molecule-1 - chemistry; Intercellular Adhesion Molecule-1 - physiology; Intercellular Adhesion Molecule-1 - ultrastructure; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; receptor specificity; Receptors, Virus - chemistry; Receptors, Virus - physiology; Receptors, Virus - ultrastructure; Rhinovirus; Rhinovirus - chemistry; Rhinovirus - physiology; Rhinovirus - ultrastructure; rhinoviruses; Serotyping; Software; Static Electricity
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1093/emboj/18.22.6249

Two human rhinovirus serotypes complexed with two‐ and five‐domain soluble fragments of the cellular receptor, intercellular adhesion molecule‐1, have been investigated by X‐ray crystallographic analyses of the individual components and by cryo‐electron microscopy of the complexes. The three‐dimensional image reconstructions provide a molecular envelope within which the crystal structures of the viruses and the receptor fragments can be positioned with accuracy. The N‐terminal domain of the receptor binds to the rhinovirus ‘canyon’ surrounding the icosahedral 5‐fold axes. Fitting of molecular models into the image reconstruction density identified the residues on the virus that interact with those on the receptor surface, demonstrating complementarity of the electrostatic patterns for the tip of the N‐terminal receptor domain and the floor of the canyon. The complexes seen in the image reconstructions probably represent the first stage of a multistep binding process. A mechanism is proposed for the subsequent viral uncoating process.