Induced expression and localization to nuclear-inclusion bodies of hsp70 in varicella-zoster virus-infected human diploid fibroblasts.

Abstract

The expression and subcellular localization of cellular heat-shock protein hsp70 were examined in varicella-zoster virus (VZV)-infected human diploid fibroblasts. Infection with VZV elevated the steady-state levels of hsp70 mRNA by 24 hr post-infection (hpi). Western blotting analysis revealed an increase in accumulation of hsp70 from 24 hpi. Subcellular localization of the hsp70 in VZV-infected cells was examined by indirect immunofluorescence. In most VZV-infected cells, hsp70 was localized to inclusion bodies induced in the cell nucleus by infection with VZV. In some cells, however, the remaining parts of the cell nucleus and the cytoplasm were also stained with anti-hsp70 antibody. These results indicate that infection with VZV induces the expression of hsp70 and its localization to VZV-specific inclusion bodies, which suggests the involvement of hsp70 in molecular events within inclusion bodies.