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.

TitleReplacement 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.
Publication TypeJournal Article
Year of Publication1997
AuthorsTyler JK, Orr A, Everett RD
JournalJ Gen Virol
Volume78 ( Pt 1)
Pagination179-88
Date Published1997 Jan
ISSN0022-1317
KeywordsAnimals, Cell Line, Chloramphenicol O-Acetyltransferase, Chlorocebus aethiops, Cricetinae, DNA-Binding Proteins, Genes, Viral, HeLa Cells, Herpesvirus 1, Human, Herpesvirus 3, Human, Humans, Immediate-Early Proteins, Kidney, Polymerase Chain Reaction, Protein Multimerization, Recombinant Fusion Proteins, Restriction Mapping, Transfection, Vero Cells
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.

DOI10.1099/0022-1317-78-1-179
Alternate JournalJ Gen Virol
PubMed ID9010302
Related Faculty: 
Jessica K. Tyler, Ph.D.

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