Disease relevance of UL47

• The gene products of herpes simplex virus type 1 UL46 and UL47 enhance the efficiency of alpha TIF (VP16)-mediated alpha gene expression through an unknown mechanism of action [1].
• The ORF 3 encoded a predicted protein of 601 aa (M(r) 67.5 kDa) which exhibited limited homology (18% overall identity) with the UL47 protein (major tegument protein) of HSV-1 [2].
• Sequence analysis of a lambda gt11 insert of equine herpesvirus 1 gp10 identified an open reading frame in equine herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus [3].
• The most abundant protein in bovine herpes 1 virions is a homologue of herpes simplex virus type 1 UL47 [4].
• Previous studies with transfected cells have shown that the herpes simplex virus type 1 (HSV-1) and bovine herpesvirus 1 (BHV-1) UL47 proteins shuttle between the nucleus and the cytoplasm [5].

High impact information on UL47

• Furthermore, we demonstrate that actinomycin D inhibits the reaccumulation of UL47 in the nuclei of infected cells [5].
• Herpes simplex virus type 1 UL46 and UL47 deletion mutants lack VP11 and VP12 or VP13 and VP14, respectively, and exhibit altered viral thymidine kinase expression [1].
• This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47 [3].
• In infected V2.6 cells, the levels of late gC and UL47 mRNA were 7- to 12-fold lower than those of infected Vero cells under conditions where the levels of viral DNA replication in these two cell types were similar [6].
• To determine if the negative effect of d105 ICP8 on the late gene expression was exerted at the transcriptional level, we measured the levels of mRNAs and transcription from three late genes, gC, UL47, and gD, in V2.6 cells and Vero cells infected with the HSV-1 wild-type virus [6].

Biological context of UL47

• The primary structure of VP8 showed considerable homology with the product of the UL47 reading frame of herpes simplex virus type 1 [4].
• The absence of UL47 reduces by up to 80% the ability of the virus to induce an alpha-regulated thymidine kinase reporter gene resident in 143TK- cells [7].
• The synthesis and phosphorylation of these proteins were inhibited by AG17, and suppression of ICP 19/20, which were identified as the UL47 gene products, was the greatest [8].

Associations of UL47 with chemical compounds

• UL47 regulation was investigated using phosphonoacetic acid (PAA), an inhibitor of DNA synthesis: the amounts of the 82/81K protein synthesized were compared with those of 65KDBP, an early gene product, and 21K/22K, a true late gene product [9].

References