Replacement of the herpes simplex virus type 1 Vmw175 DNA binding domain with its varicella-zoster virus counterpart results in a protein with novel regulatory properties that can support virus growth. Academic Article uri icon

Overview

abstract

  • The alphaherpesviruses encode major immediate early transactivator proteins that are essential for the expression of later classes of viral genes. We have previously shown that the extensive sequence similarity between the herpes simplex virus type 1 (HSV-1) and varicella-zoster virus (VZV) members of the family (proteins Vmw175 and VZV140k) extends to function, since a virus which expresses VZV140k in place of Vmw175 is able to grow, albeit at reduced efficiency. We have also shown that the DNA binding characteristics of the isolated DNA binding domains of Vmw175 and VZV140k are related but distinct. In order to assess whether the different DNA binding properties of the two proteins are responsible for the differences in their individual transcriptional regulatory functions, we constructed a plasmid and an HSV-1 virus in which the VZV140k DNA binding domain coding sequences replace those of Vmw175. The characteristics of the resultant hybrid protein in transfection assays and during virus infection suggest that the nature of the DNA binding domain plays a significant role in the transactivation and repression properties of the Vmw1 75 family of proteins.

publication date

  • January 1, 1997

Research

keywords

  • DNA-Binding Proteins
  • Herpesvirus 1, Human
  • Herpesvirus 3, Human
  • Immediate-Early Proteins

Identity

Scopus Document Identifier

  • 0031022121

Digital Object Identifier (DOI)

  • 10.1099/0022-1317-78-1-179

PubMed ID

  • 9010302

Additional Document Info

volume

  • 78 ( Pt 1)