Chromy Laura R, Oltman Amy, Estes Patricia A, Garcea Robert L
University of Colorado Health Sciences Center, Aurora, CO 80045, USA.
J Virol. 2006 May;80(10):5086-91. doi: 10.1128/JVI.80.10.5086-5091.2006.
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 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.
热休克蛋白70（Hsp70）伴侣蛋白在多瘤病毒和乳头瘤病毒组装过程中发挥作用，病毒感染后期其在体内与多瘤病毒衣壳蛋白的相互作用以及在体外将病毒衣壳粒组装成衣壳的能力都证明了这一点。我们研究了Hsp70伴侣蛋白是否也可能参与脱壳反应。在体内，感染小鼠细胞3小时后，Hsp70与多瘤病毒病毒体VP1共免疫沉淀。在体外，原核和真核Hsp70伴侣蛋白在能量依赖反应中有效地拆解了多瘤病毒和乳头瘤病毒样颗粒及病毒体。这些观察结果支持细胞伴侣蛋白在这些病毒拆解过程中发挥作用。
