Skip to main content
Figure 7 | Virology Journal

Figure 7

From: Herpes simplex virus type 1 UL14 tegument protein regulates intracellular compartmentalization of major tegument protein VP16

Figure 7

Aggresome formation in UL14D-VP16GFP-infected virus, and protein quality control components in infected cells. HEP-2 cells were infected with wild-type and UL14D virus at an MOI of 3. Cells were fixed at the indicated time points, permeabilized and stained with anti-vimentin, anti-Hsp70, and anti-protesome 20S subunit. VP16GFP localized to aggresomes surrounded by a vimentin cage in UL14D-infected cells (D-F), but the filamentous structure of vimentin was maintained in the UL14R-infected cells (B). At 10 h.p.i. when no aggresomes were detected in the UL14D-infected cells, the proteasome and Hsp70 localized to distinct punctate structures that partially colocalized with the VP16GFP foci in both Ul14R- and UL14D- infected cells (G-J, K-N). The VP16GFP foci localized to the periphery of cell nuclei (K-N). At 18 h.p.i. the VICE domains appeared in UL14R-infected cells, and substantial fractions of both the proteasome and Hsp70 localized to the nucleus (O-R). In cells infected with UL14D-VP16GFP, both the proteasome and Hsp70 were distributed in the cytoplasm and nuclei, and there was colocalization of Hsp70 and the proteasome with VP16GFP in the aggresomes (S-V).

Back to article page