Chaperone-mediated in vitro disassembly of polyoma- and papillomaviruses.
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 co-immunoprecipitated 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.
Chromy
Laura R
LR
University of Colorado Health Sciences Center, Aurora, CO 80045, USA.
Oltman
Amy
A
Estes
Patricia A
PA
Garcea
Robert L
RL
D000818:Animals; D052688:Bovine papillomavirus 1 / Q000378:metabolism / Q000502:physiology; D036022:Capsid Proteins / Q000378:metabolism / Q000502:physiology; D002417:Cattle; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology*; D066298:In Vitro Techniques; D051379:Mice; D041681:NIH 3T3 Cells; D011120:Polyomavirus / Q000378:metabolism / Q000502:physiology; D014771:Virion / Q000378:metabolism / Q000502:physiology; D019065:Virus Assembly / Q000502:physiology*
D036022:Capsid Proteins; D018840:HSP70 Heat-Shock Proteins; C062481:VP1 protein, polyomavirus