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Journal of Virology, June 2001, p. 4984-4989, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.4984-4989.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Kinetic Analysis of the Effect of Poliovirus Receptor on Viral Uncoating: the Receptor as a Catalyst

Simon K. Tsang,1 Brian M. McDermott,2 Vincent R. Racaniello,2 and James M. Hogle1,3,*

Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts 021381; Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, New York 100322; and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021153

Received 2 November 2000/Accepted 6 March 2001

We examined the role of soluble poliovirus receptor on the transition of native poliovirus (160S or N particle) to an infectious intermediate (135S or A particle). The viral receptor behaves as a classic transition state theory catalyst, facilitating the N-to-A conversion by lowering the activation energy for the process by 50 kcal/mol. In contrast to earlier studies which demonstrated that capsid-binding drugs inhibit thermally mediated N-to-A conversion through entropic stabilization alone, capsid-binding drugs are shown to inhibit receptor-mediated N-to-A conversion through a combination of enthalpic and entropic effects.

* Corresponding author. Mailing address: Department of Biological Chemistry, and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115. Phone: (617) 432-3919. Fax: (617) 432-4360. E-mail: hogle{at}hogles.med.harvard.edu.

Journal of Virology, June 2001, p. 4984-4989, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.4984-4989.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.