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J Virol, July 1998, p. 6244-6246, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Domain Structure of ICAM-1 and the Kinetics of Binding to Rhinovirus

José M. Casasnovas, Joanna K. Bickford, and Timothy A. Springer*

The Center for Blood Research and Harvard Medical School Department of Pathology, Boston, Massachusetts

Received 10 November 1997/Accepted 9 April 1998

Fragments of intercellular adhesion molecule 1 (ICAM- 1) containing only the two most N terminal of its five immunoglobulin SF domains bind to rhinovirus 3 with the same affinity and kinetics as a fragment with the entire extracellular domain. The fully active two-domain fragments contain 5 or 14 more residues than a previously described fragment that is only partially active. Comparison of X-ray crystal structures show differences at the bottom of domain 2. Four different glycoforms of ICAM- 1 bind with identical kinetics.

* Corresponding author. Mailing address: The Center for Blood Research and Harvard Medical School Department of Pathology, 200 Longwood Avenue, Boston, MA 02115. Phone: (617) 278-3200. Fax: (617) 278-3232. E-mail: springer{at}sprsgi.med.harvard.edu.

J Virol, July 1998, p. 6244-6246, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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