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Xiao, C, Bator-Kelly, CM, Rieder, E, Chipman, PR, Craig, A, Kuhn, RJ, Wimmer, E and Rossmann, MG (2005) The crystal structure of coxsackievirus A21 and its interaction with ICAM-1. Structure 13:1019-33

CVA21 and polioviruses both belong to the Enterovirus genus in the family of Picornaviridae, whereas rhinoviruses form a distinct picornavirus genus. Nevertheless, CVA21 and the major group of human rhinoviruses recognize intercellular adhesion molecule-1 (ICAM-1) as their cellular receptor, whereas polioviruses use poliovirus receptor. The crystal structure of CVA21 has been determined to 3.2 A resolution. Its structure has greater similarity to poliovirus structures than to other known picornavirus structures. Cryo-electron microscopy (cryo-EM) was used to determine an 8.0 A resolution structure of CVA21 complexed with an ICAM-1 variant, ICAM-1(Kilifi). The cryo-EM map was fitted with the crystal structures of ICAM-1 and CVA21. Significant differences in the structure of CVA21 with respect to the poliovirus structures account for the inability of ICAM-1 to bind polioviruses. The interface between CVA21 and ICAM-1 has shape and electrostatic complementarity with many residues being conserved among those CVAs that bind ICAM-1.

PubMed Online version:10.1016/j.str.2005.04.011

Amino Acid Sequence; Capsid; Cryoelectron Microscopy; Crystallography, X-Ray; Dimerization; Enterovirus/metabolism; Humans; Intercellular Adhesion Molecule-1/chemistry; Ions; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Sequence Homology, Amino Acid; Static Electricity