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Originally published In Press as doi:10.1074/jbc.M002146200 on April 18, 2000

J. Biol. Chem., Vol. 275, Issue 30, 23089-23096, July 28, 2000
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Two Distinct Binding Affinities of Poliovirus for Its Cellular Receptor*

Brian M. McDermott Jr.Dagger , Ann H. Rux§||, Roselyn J. Eisenberg§||, Gary H. Cohen§, and Vincent R. RacanielloDagger **

From the Dagger  Department of Microbiology, Columbia University College of Physicians & Surgeons, New York, New York 10032 and the § Department of Microbiology and  Center for Oral Health Research, School of Dental Medicine, and || Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

To study the kinetics and equilibrium of poliovirus binding to the poliovirus receptor, we used surface plasmon resonance to examine the interaction of a soluble form of the receptor with poliovirus. Soluble receptor purified from mammalian cells is able to bind poliovirus, neutralize viral infectivity, and induce structural changes in the virus particle. Binding studies revealed that there are two binding sites for the receptor on the poliovirus type 1 capsid, with affinity constants at 20 °C of KD1 = 0.67 µM and KD2 = 0.11 µM. The relative abundance of the two binding sites varies with temperature. At 20 °C, the KD2 site constitutes approximately 46% of the total binding sites on the sensor chip, and its relative abundance decreased with decreasing temperature such that at 5 °C, the relative abundance of the KD2 site is only 12% of the total binding sites. Absolute levels of the KD1 site remained relatively constant at all temperatures tested. The two binding sites may correspond to docking sites for domain 1 of the receptor on the viral capsid, as predicted by a model of the poliovirus-receptor complex. Alternatively, the binding sites may be a consequence of structural breathing, or could result from receptor-induced conformational changes in the virus.

* This work was supported by Public Health Service Grant AI20017 (to V. R. R.) from the NIAID, National Institutes of Health, and NINDS Grants NS-30606 and NS-36731 from the National Institutes of Health (to R. J. E. and G. H. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Dept. of Microbiology, Columbia University College of Physicians & Surgeons, 701 W. 168th St., New York, NY 10032. Tel.: 212-305-5707; Fax: 212-305-5106; E-mail: vrr1@columbia.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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