The crystal structure of coxsackievirus A21 and its interaction with ICAM-1.
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.
Xiao
Chuan
C
Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907, USA.
Bator-Kelly
Carol M
CM
Rieder
Elizabeth
E
Chipman
Paul R
PR
Craig
Alister
A
Kuhn
Richard J
RJ
Wimmer
Eckard
E
Rossmann
Michael G
MG
D000595:Amino Acid Sequence; D002213:Capsid; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D019281:Dimerization; D004770:Enterovirus / Q000378:metabolism*; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000737:chemistry*; D007477:Ions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity
D007477:Ions; D018799:Intercellular Adhesion Molecule-1