Picornavirus–receptor interactions

• Published in: Trends in Microbiology 2002-07, Vol.10 (7), p.324-331
• Main Authors: Rossmann, Michael G., He, Yongning, Kuhn, Richard J.
• Format: Article
• Language: English
• Subjects: Animals; Coxsackie and Adenovirus Receptor-Like Membrane Protein; coxsackievirus; cryoelectron microscopy; enterovirus; Enterovirus B, Human - metabolism; Humans; ICAM-1; Ig superfamily; Immunoglobulins - metabolism; Intercellular Adhesion Molecule-1 - metabolism; Picornaviridae - metabolism; pocket factor; poliovirus; Receptors, Virus - metabolism; rhinovirus; viral canyon; viral receptors
• ISSN: 0966-842X; 1878-4380
• DOI: 10.1016/S0966-842X(02)02383-1

Many picornaviruses use cell-surface molecules belonging to the immunoglobulin superfamily (IgSF) as their cellular receptors. These molecules usually consist of tandem repeats of between two and five Ig-like domains whose amino-terminal domains (D1) interact with invading viruses, with their carboxy-terminal sections comprising a transmembrane and a short cytoplasmic region. Most rhino- and enteroviruses, belonging to the Picornavirus family, use a canyon-like feature on their surface to attach to cellular receptors. Binding into the canyon destabilizes the virus and thus initiates the uncoating process. By contrast, non-IgSF molecules, when used by picornaviruses as receptors, bind outside the canyon and do not cause viral instability. Many picornaviruses attach to cellular receptors using a canyon-like region on their surface and it is proposed that the binding of receptors in the canyon initiates viral uncoating. It is hoped that analysis of virus-receptor interactions using high-resolution cryo-electron microscopy will reveal more about the mechanisms involved in this process.