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Journal of Virology, September 2004, p. 10034-10044, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.10034-10044.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Discrimination among Rhinovirus Serotypes for a Variant ICAM-1 Receptor Molecule

Chuan Xiao,1 Tobias J. Tuthill,2 Carol M. Bator Kelly,1 Lisa J. Challinor,2 Paul R. Chipman,1 Richard A. Killington,2 David J. Rowlands,2 Alister Craig,3 and Michael G. Rossmann1*

Department of Biological Sciences, Purdue University, West Lafayette, Indiana,1 School of Biochemistry and Microbiology, University of Leeds, Leeds,2 Liverpool School of Tropical Medicine, Liverpool, United Kingdom3

Received 13 February 2004/ Accepted 7 May 2004

Intercellular adhesion molecule 1 (ICAM-1) is the cellular receptor for the major group of human rhinovirus serotypes, including human rhinovirus 14 (HRV14) and HRV16. A naturally occurring variant of ICAM-1, ICAM-1Kilifi, has altered binding characteristics with respect to different HRV serotypes. HRV14 binds to ICAM-1 only transiently at physiological temperatures but forms a stable complex with ICAM-1Kilifi. Conversely, HRV16 forms a stable complex with ICAM-1 but does not bind to ICAM-1Kilifi. The three-dimensional structures of HRV14 and HRV16, complexed with ICAM-1, and the structure of HRV14, complexed with ICAM-1Kilifi, have been determined by cryoelectron microscopy (cryoEM) image reconstruction to a resolution of approximately 10 Å. Structures determined by X-ray crystallography of both viruses and of ICAM-1 were fitted into the cryoEM density maps. The interfaces between the viruses and receptors contain extensive ionic networks. However, the interactions between the viruses and ICAM-1Kilifi contain one less salt bridge than between the viruses and ICAM-1. As HRV16 has fewer overall interactions with ICAM-1 than HRV14, the absence of this charge interaction has a greater impact on the binding of ICAM-1Kilifi to HRV16 than to HRV14.

* Corresponding author. Mailing address: Department of Biological Sciences, Purdue University, 915 W. State St., West Layfayette, IN 47909-2054. Phone: (765) 494-4911. Fax: (765) 496-1189. E-mail: mgr{at}indiana.bio.purdue.edu.

Journal of Virology, September 2004, p. 10034-10044, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.10034-10044.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.





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