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Journal of Virology, October 2008, p. 9848-9857, Vol. 82, No. 20
0022-538X/08/$08.00+0     doi:10.1128/JVI.01221-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Possible Role for Cellular Karyopherins in Regulating Polyomavirus and Papillomavirus Capsid Assembly {triangledown}

Gregory Bird,1 Malinda O'Donnell,1 Junona Moroianu,2 and Robert L. Garcea1*

Department of Pediatrics, University of Colorado School of Medicine, UCHSC at Fitzsimons RC1-North, Room 4100, Mail Stop 8302, P.O. Box 6511, Aurora, Colorado 80045,1 Biology Department, Boston College, 140 Commonwealth Avenue, Chestnut Hill, Massachusetts 02467-38112

Received 12 June 2008/ Accepted 5 August 2008

Polyomavirus and papillomavirus (papovavirus) capsids are composed of 72 capsomeres of their major capsid proteins, VP1 and L1, respectively. After translation in the cytoplasm, L1 and VP1 pentamerize into capsomeres and are then imported into the nucleus using the cellular {alpha} and β karyopherins. Virion assembly only occurs in the nucleus, and cellular mechanisms exist to prevent premature capsid assembly in the cytosol. We have identified the karyopherin family of nuclear import factors as possible "chaperones" in preventing the cytoplasmic assembly of papovavirus capsomeres. Recombinant murine polyomavirus (mPy) VP1 and human papillomavirus type 11 (HPV11) L1 capsomeres bound the karyopherin heterodimer {alpha}2β1 in vitro in a nuclear localization signal (NLS)-dependent manner. Because the amino acid sequence comprising the NLS of VP1 and L1 overlaps the previously identified DNA binding domain, we examined the relationship between karyopherin and DNA binding of both mPy VP1 and HPV11 L1. Capsomeres of L1, but not VP1, bound by karyopherin {alpha}2β1 or β1 alone were unable to bind DNA. VP1 and L1 capsomeres could bind both karyopherin {alpha}2 and DNA simultaneously. Both VP1 and L1 capsomeres bound by karyopherin {alpha}2β1 were unable to assemble into capsids, as shown by in vitro assembly reactions. These results support a role for karyopherins as chaperones in the in vivo regulation of viral capsid assembly.

* Corresponding author. Mailing address: Department of Pediatrics, University of Colorado School of Medicine, UCHSC at Fitzsimons RC1-North, Room 4100, Mail Stop 8302, P.O. Box 6511, Aurora, CO 80045. Phone: (303) 492-1669. Fax: (303) 492-1133. E-mail: Robert.garcea{at}colorado.edu

{triangledown} Published ahead of print on 13 August 2008.

Journal of Virology, October 2008, p. 9848-9857, Vol. 82, No. 20
0022-538X/08/$08.00+0     doi:10.1128/JVI.01221-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Erickson, K. D., Garcea, R. L., Tsai, B. (2009). Ganglioside GT1b Is a Putative Host Cell Receptor for the Merkel Cell Polyomavirus. J. Virol. 83: 10275-10279 [Abstract] [Full Text]  
  • Conway, M.J., Meyers, C. (2009). Replication and Assembly of Human Papillomaviruses. JDR 88: 307-317 [Abstract] [Full Text]  


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