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Journal of Virology, April 2000, p. 3929-3931, Vol. 74, No. 8
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

An Antiviral Compound That Blocks Structural Transitions of Poliovirus Prevents Receptor Binding at Low Temperatures

Alan W. Dove and Vincent R. Racaniello*

Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, New York 10032

Received 3 September 1999/Accepted 24 January 2000

Drugs such as WIN51711 that inhibit picornavirus replication are thought to block poliovirus infectivity by binding to the capsid and preventing structural transitions required for uncoating. We examined the activity of WIN51711 at temperatures where capsid flexibility is thought to be decreased. Below 37°C, WIN51711 inhibits the binding of wild-type poliovirus to cells but does not affect the binding of a poliovirus mutant which is believed to undergo structural transitions more readily. These results suggest that the poliovirus capsid must undergo structural changes to bind to its cellular receptor.


* Corresponding author. Mailing address: Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 W. 168th St., New York, NY 10032. Phone: (212) 305-5707. Fax: (212) 305-5106. E-mail: vrr1{at}columbia.edu.


Journal of Virology, April 2000, p. 3929-3931, Vol. 74, No. 8
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



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