Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3424418 | Virology | 2012 | 10 Pages |
The amino acid sequence of the UL31 protein (UL31P) of equine herpesvirus 1 (EHV-1) has homology to that of the ICP8 of herpes simplex virus type 1 (HSV-1). Here we show that the UL31 gene is synergistically trans-activated by the IEP and the UL5P (EICP27). Detection of the UL31 RNA transcript and the UL31P in EHV-1-infected cells at 6 h post-infection (hpi) as well as metabolic inhibition assays indicated that UL31 is an early gene. The UL31P preferentially bound to single-stranded DNA over double-stranded DNA in gel shift assays. Subcellular localization of the green fluorescent protein (GFP)–UL31 fusion proteins revealed that the C-terminal 32 amino acid residues of the UL31P are responsible for the nuclear localization. These findings may contribute to defining the role of the UL31P single-stranded DNA-binding protein in EHV-1 DNA replication.
► We determined the molecular properties of the EHV-1 UL31 gene. ► The UL31 gene is an early gene that is synergistically trans-activated by the IEP and the UL5P. ► The UL31P is a single-stranded DNA-binding protein. ► The UL31P has a nuclear localization signal sequence at the C-terminal 32 amino acid residues.