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Journal of Virology, December 2007, p. 12996-13004, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01037-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

A Chaperone-Activated Nonenveloped Virus Perforates the Physiologically Relevant Endoplasmic Reticulum Membrane{triangledown}

Emily K. Rainey-Barger, Brian Magnuson, and Billy Tsai*

Department of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, Rm. 3043, Ann Arbor, Michigan 48109

Received 12 May 2007/ Accepted 11 September 2007

The nonenveloped polyomavirus (Py) traffics from the plasma membrane to the endoplasmic reticulum (ER), where it penetrates the ER membrane, allowing the viral genome to reach the nucleus to cause infection. The mechanism of membrane penetration for Py, and for other nonenveloped viruses, remains poorly characterized. We showed previously that the ER chaperone ERp29 alters the conformation of Py coat protein VP1, enabling the virus to interact with membranes. Here, we developed a membrane perforation assay and showed that the ERp29-activated Py perforates the physiologically relevant ER membrane, an event that likely initiates viral penetration. Biochemical analysis revealed that the internal protein VP2 is exposed in the activated viral particle. Accordingly, we demonstrate that VP2 binds to, integrates into, and perforates the ER membrane; the other internal protein, VP3, binds to and integrates into the ER membrane but is not sufficient for perforation. Our data thus link the activity of a cellular factor on a nonenveloped virus to the membrane perforation event and identify a viral component that mediates this process.

* Corresponding author. Mailing address: Department of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, Rm. 3043, Ann Arbor, MI 48109. Phone: (734) 764-4167. Fax: (734) 764-5155. E-mail: btsai{at}umich.edu

{triangledown} Published ahead of print on 19 September 2007.

Journal of Virology, December 2007, p. 12996-13004, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01037-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rainey-Barger, E. K., Mkrtchian, S., Tsai, B. (2009). The C-Terminal Domain of ERp29 Mediates Polyomavirus Binding, Unfolding, and Infection. J. Virol. 83: 1483-1491 [Abstract] [Full Text]  


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