The herpes simplex virus pUL16 and pUL21 proteins prevent capsids from docking at nuclear pore complexes

After entry into cells, herpes simplex virus (HSV) nucleocapsids dock at nuclear pore complexes (NPCs) through which viral genomes are released into the nucleoplasm where viral gene expression, genome replication, and early steps in virion assembly take place. After their assembly, nucleocapsids are translocated to the cytoplasm for final virion maturation. Nascent cytoplasmic nucleocapsids are prevented from binding to NPCs and delivering their genomes to the nucleus from which they emerged, but how this is accomplished is not understood. Here we report that HSV pUL16 and pUL21 deletion mutants accumulate empty capsids at the cytoplasmic face of NPCs late in infection. Additionally, prior expression of pUL16 and pUL21 prevented incoming nucleocapsids from docking at NPCs, delivering their genomes to the nucleus and initiating viral gene expression. Both pUL16 and pUL21 localized to the nuclear envelope, placing them in an appropriate location to interfere with nucleocapsid/NPC interact..., , , # Research data

Confocal and TEM images associated with The Herpes Simplex Virus pUL16 and pUL21 Proteins Prevent Capsids from Docking at Nuclear Pore Complexes

## Description of the data and file structure

Folders are named with corresponding figure numbers. File types include .oib, .jpg and .tif. All can be opened with NIH Image/Fiji.

Figure 2D: The localization of HSV-2 and HSV-1 capsids in the absence of pUL16 and/or pUL21. The confocal images of Vero cells in this folder were used for quantification of the percentage of HSV-1 infected cells with capsids accumulated at the nuclear envelope. Three biological replicates with n = 198–258 infected cells examined per biological replicate. Subfolder titles correspond to the different virus strains analyzed.

Figure 3E: The colocalization of HSV-2 capsids with NPCs at late times in infection. The electron micrographs of Vero cells in this folder were used for quantification of the number of A-capsids docked at NPCs per nuclear section....,