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Journal of Virology, May 2006, p. 5086-5091, Vol. 80, No. 10
0022-538X/06/$08.00+0 doi:10.1128/JVI.80.10.5086-5091.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Amy Oltman,
Patricia A. Estes, and
Robert L. Garcea*
Section of Pediatric Hematology/Oncology and Molecular Biology Program, University of Colorado Health Sciences Center, Aurora, Colorado 80045
Received 15 November 2005/ Accepted 20 February 2006
Hsp70 chaperones play a role in polyoma- and papillomavirus assembly, as evidenced by their interaction in vivo with polyomavirus capsid proteins at late times after virus infection and by their ability to assemble viral capsomeres into capsids in vitro. We studied whether Hsp70 chaperones might also participate in the uncoating reaction. In vivo, Hsp70 coimmunoprecipitated with polyomavirus virion VP1 at 3 h after infection of mouse cells. In vitro, prokaryotic and eukaryotic Hsp70 chaperones efficiently disassembled polyoma- and papillomavirus-like particles and virions in energy-dependent reactions. These observations support a role for cell chaperones in the disassembly of these viruses.
Present address: University of Michigan School of Medicine, 1301 Catherine Street, Ann Arbor, MI 48109-0611.
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