Journal of Virology, March 2001, p. 2444-2451, Vol. 75, No. 5
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.5.2444-2451.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392,1 and Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York, Stony Brook, New York 11794-52222
Received 15 September 2000/Accepted 28 November 2000
Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a causative agent of the common cold. It uses the same cellular receptor, intercellular adhesion molecule 1 (ICAM-1), as does the major group of HRVs; unlike HRVs, however, it is stable at acid pH. The cryoelectron microscopy (cryoEM) image reconstruction of CAV21 is consistent with the highly homologous crystal structure of poliovirus 1; like other enteroviruses and HRVs, CAV21 has a canyon-like depression around each of the 12 fivefold vertices. A cryoEM reconstruction of CAV21 complexed with ICAM-1 shows all five domains of the extracellular component of ICAM-1. The known atomic structure of the ICAM-1 amino-terminal domains D1 and D2 has been fitted into the cryoEM density of the complex. The site of ICAM-1 binding within the canyon of CAV21 overlaps the site of receptor recognition utilized by rhinoviruses and polioviruses. Interactions within this common region may be essential for triggering viral destabilization after attachment to susceptible cells.
Present address: School of Biological Sciences, University of
Manchester, Manchester M13 9PT, England.
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