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Journal of Virology, February 2000, p. 1342-1354, Vol. 74, No. 3
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Molecular Tectonic Model of Virus Structural Transitions: the Putative Cell Entry States of Poliovirus

David M. Belnap,1 David J. Filman,2 Benes L. Trus,1,3 Naiqian Cheng,1 Frank P. Booy,1,dagger James F. Conway,1 Stephen Curry,2,Dagger Chaitanya N. Hiremath,2,§ Simon K. Tsang,4 Alasdair C. Steven,1 and James M. Hogle2,4,*

Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases,1 and Computational Bioscience and Engineering Laboratory, Center for Information Technology,3 National Institutes of Health, Bethesda, Maryland 20892; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152; and Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts 021384

Received 4 August 1999/Accepted 19 October 1999

Upon interacting with its receptor, poliovirus undergoes conformational changes that are implicated in cell entry, including the externalization of the viral protein VP4 and the N terminus of VP1. We have determined the structures of native virions and of two putative cell entry intermediates, the 135S and 80S particles, at ~22-Å resolution by cryo-electron microscopy. The 135S and 80S particles are both ~4% larger than the virion. Pseudoatomic models were constructed by adjusting the beta-barrel domains of the three capsid proteins VP1, VP2, and VP3 from their known positions in the virion to fit the 135S and 80S reconstructions. Domain movements of up to 9 Å were detected, analogous to the shifting of tectonic plates. These movements create gaps between adjacent subunits. The gaps at the sites where VP1, VP2, and VP3 subunits meet are plausible candidates for the emergence of VP4 and the N terminus of VP1. The implications of these observations are discussed for models in which the externalized components form a transmembrane pore through which viral RNA enters the infected cell.

* Corresponding author. Mailing address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115. Phone: (617) 432-3918. Fax: (617) 432-4360. E-mail: hogle{at}hogles.med.harvard.edu.

dagger Present address: Department of Biochemistry, Wolfson Laboratory, Imperial College, London SW7 1AY, United Kingdom.

Dagger Present address: Biophysics Group, Blackett Laboratory, Imperial College, London SW7 2BZ, United Kingdom.

§ Present address: Fresenius Medical Care North America, Lexington, MA 02420.

Journal of Virology, February 2000, p. 1342-1354, Vol. 74, No. 3
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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