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The crystal structure of coxsackievirus A21 and its interaction with ICAM-1

Xiao, C. A., Bator-Kelly, C. M., Rieder, E., Chipman, P. R., Craig, Alister ORCID: https://orcid.org/0000-0003-0914-6164, Kuhn, R. J., Wimmer, E. and Rossmann, M. G. (2005) 'The crystal structure of coxsackievirus A21 and its interaction with ICAM-1'. Structure, Vol 13, Issue 7, pp. 1019-1033.

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Abstract

CVA21 and polloviruses 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 angstrom 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 angstrom 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.

Item Type: Article
Uncontrolled Keywords: intercellular-adhesion molecule-1 decay-accelerating factor cellular receptor interactions common cold virus human rhinovirus-14 3-dimensional structure angstrom resolution factor cd55 poliovirus protein
Subjects: QU Biochemistry > Cells and Genetics > QU 300 General works
QU Biochemistry > Cells and Genetics > QU 350 Cellular structures
QU Biochemistry > QU 4 General works
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI): https://doi.org/10.1016/j.str.2005.04.011
Depositing User: Sarah Lewis-Newton
Date Deposited: 17 Oct 2011 14:46
Last Modified: 06 Feb 2018 13:03
URI: http://archive.lstmed.ac.uk/id/eprint/1958

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