Title | The crystal structure of coxsackievirus A21 and its interaction with ICAM-1. | ||
Author | Xiao, Chuan; Bator-Kelly, Carol M; Rieder, Elizabeth; Chipman, Paul R; Craig, Alister; Kuhn, Richard J; Wimmer, Eckard; Rossmann, Michael G | ||
Journal | Structure | Publication Year/Month | 2005-Jul |
PMID | 16004874 | PMCID | -N/A- |
Affiliation | 1.Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA. |
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.