title: Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 produces a phenotype similar to that of the in1814 linker insertion mutation.
abstract: We examined the phenotype of a herpes simplex virus (HSV) type 1 mutant (V422) in which the C-terminal acidic activation domain of the virion transactivator VP16 is truncated at residue 422. The efficiency of plaque formation by V422 on Vero cells was boosted by approximately 100-fold by including hexamethylene bis-acetimide (HMBA) in the growth medium, as previously observed with the in1814 VP16 linker insertion mutant isolated by Preston and colleagues. V422 displayed severely reduced levels of the immediate-early transcripts encoding ICP0 and ICP4 during infection in the presence of cycloheximide, and this defect was partially overcome by the addition of HMBA. The defect in plaque formation exhibited by V422 and in 1814 was efficiently complemented in U2OS osteosarcoma cells, which had previously been shown to complement ICP0 null mutations. Taken in combination, these data confirm the key role of VP16 in triggering the onset of the HSV lytic cycle.
authors.affiliation: Institute for Molecular Biology and Biotechnology, Pathology Department, McMaster University, Hamilton, Ontario, Canada. Jim.Smiley@ualberta.ca
authors.forename: J R
authors.initials: JR
authors.lastname: Smiley
authors.forename: J
authors.initials: J
authors.lastname: Duncan
mesh_terms: D000818:Animals; D002522:Chlorocebus aethiops; D017405:Herpes Simplex Virus Protein Vmw65 / Q000737:chemistry / Q000502:physiology*; D017874:Immediate-Early Proteins / Q000235:genetics; D009154:Mutation; D010641:Phenotype; D011401:Promoter Regions, Genetic; D015533:Transcriptional Activation; D044767:Ubiquitin-Protein Ligases; D014709:Vero Cells
chemical_list: D017405:Herpes Simplex Virus Protein Vmw65; D017874:Immediate-Early Proteins; C048925:herpes simplex virus, type 1 protein ICP4; D044767:Ubiquitin-Protein Ligases; C051804:Vmw110 protein, Human herpesvirus 1