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Journal of Virology, June 2005, p. 7745-7755, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7745-7755.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Structure of the Poliovirus 135S Cell Entry Intermediate at 10-Angstrom Resolution Reveals the Location of an Externalized Polypeptide That Binds to Membranes{dagger}

Doryen Bubeck,1 David J. Filman,1 Naiqian Cheng,2 Alasdair C. Steven,2 James M. Hogle,1* and David M. Belnap2*

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115,1 Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 208922

Received 16 December 2004/ Accepted 14 February 2005

Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational change to the 135S cell entry intermediate. This transition involves shifts of the capsid protein ß barrels, accompanied by the externalization of VP4 and the N terminus of VP1. Both polypeptides associate with membranes and are postulated to facilitate entry by forming a translocation pore for the viral RNA. We have calculated cryo-electron microscopic reconstructions of 135S particles that permit accurate placement of the ß barrels, loops, and terminal extensions of the capsid proteins. The reconstructions and resulting models indicate that each N terminus of VP1 exits the capsid though an opening in the interface between VP1 and VP3 at the base of the canyon that surrounds the fivefold axis. Comparison with reconstructions of 135S particles in which the first 31 residues of VP1 were proteolytically removed revealed that the externalized N terminus is located near the tips of propeller-like features surrounding the threefold axes rather than at the fivefold axes, as had been proposed in previous models. These observations have forced a reexamination of current models for the role of the 135S particle in transmembrane pore formation and suggest testable alternatives.

* Corresponding author. Present address for David M. Belnap: Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602. Phone: (801) 422-9163. Fax: (801) 422-0153. E-mail: David_Belnap{at}byu.edu. Mailing address for James M. Hogle: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115. Phone: (617) 432-3918. Fax: (617) 432-4360. E-mail: james_hogle{at}hms.harvard.edu.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, June 2005, p. 7745-7755, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7745-7755.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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