A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE).

Abstract

Herpes simplex virus type 1 (HSV-1) virions, contain a proteinaceous layer termed the tegument that lies between the nucleocapsid and viral envelope. Current evidence suggests that viral glycoprotein tails play a role in the recruitment of tegument-coated capsids to the site of final envelopment; vesicles derived from the trans-Golgi network. We have identified an interaction between VP22, an abundant tegument protein and the cytoplasmic tail of glycoprotein E (gE). This interaction was identified by coimmunoprecipitation studies and confirmed by a glutathione-S-transferase (GST) pulldown from infected cell lysates. Truncation mutagenesis suggests that residues 165-270 of VP22 facilitate the interaction with the cytoplasmic tail of gE. In fact, this region of VP22 is sufficient to bind to gE in the absence of additional viral proteins. Using a transfection/infection-based virion incorporation assay, residues 165-270 of VP22 fused to GFP competed efficiently with wild-type VP22 for packaging into assembling virus particles.