The herpes simplex virus type 1 transactivator ICPO mediates aberrant intracellular localization of the viral helicase/primase complex subunits.
The infected cell polypeptide 0 (ICP0) protein of herpes simplex virus type 1 (HSV-1) is a promiscuous transactivator. When expressed by transfection, ICP0 forms spherical structures in the nucleus. Using a double-label immunofluorescence assay, we have found that the HSV-1 helicase/primase complex subunits accumulate within ICP0 structures in cotransfected cells. This phenomenon was also observed in cells coexpressing ICP0 and UL6, a protein thought to be involved in the cleavage and/or packaging of viral genomes. ICP0 structures were found to be proteinaceous by immunoelectron microscopy. These results suggest that ICP0 may interact nonspecifically with a variety of viral proteins.
Lukonis
C J
CJ
Department of Microbiology MC3205, University of Connecticut Health Center, Farmington 06030, USA.
Weller
S K
SK
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002522:Chlorocebus aethiops; D004265:DNA Helicases / Q000378:metabolism*; D019915:DNA Primase; D018259:Herpesvirus 1, Human / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D017874:Immediate-Early Proteins / Q000378:metabolism*; D015534:Trans-Activators / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases; D014709:Vero Cells; D014764:Viral Proteins
D017874:Immediate-Early Proteins; D015534:Trans-Activators; D014764:Viral Proteins; D044767:Ubiquitin-Protein Ligases; C051804:Vmw110 protein, Human herpesvirus 1; D019915:DNA Primase; C062021:helicase-primase, Human herpesvirus 1; D004265:DNA Helicases