A complex formed between cell components and an HSV structural polypeptide binds to a viral immediate early gene regulatory DNA sequence

Development of herpes simplex virus replication-defective multigene vectors for combination gene therapy applications

“…Wild-type HSV contains six genes, two of which are diploid, that are transactivated immediately on infection by the tegument protein VP16 in collaboration with cellular transcription factors. 5,[48][49][50] The products of several of these IE genes (eg ICP4 and ICP22) regulate the level of expression of other IE genes and also influence transcription of cellular genes. [6][7][8]10 This suggests that any number of transgenes introduced into HSV under control of IE gene promoters could be expressed provided that either ICP0 or a functionally similar transactivator is available.…”

“…Expression of these genes is controlled by promoters containing an enhancer element responsive to the viral transactivator VP16, a structural protein which is transported into the nucleus along with the viral DNA. [3][4][5] Expression of the IE gene products initiates a cascade of viral gene expression, resulting in the synthesis first of early (E) genes which primarily encode enzyme functions required for DNA replication, followed by late (L) genes coding principally for structural components of the virion. Only two of the IE genes, ICP4 and ICP27, are essential in that their products are required for the expression of E and L genes.…”

Expression of vhs and VP16 during HSV-1 helper virus-free amplicon packaging enhances titers

“…16 VP16-mediated transcriptional activation occurs via interaction of VP16 and two cellular factors, Oct-1 [17][18][19] and HCF, 20,21 and subsequent binding of the complex to TAATGARAT elements found within HSV IE promoter regions. 22 This interaction results in robust up-regulation of IE gene expression.…”

Identification and control of the cis-acting elements of the immediate early gene of equid herpesvirus type 1

“…This is the binding site for the viral tegument protein VmW65 (also known as a-TIF and VP16) (Campbell et al, 1984;Preston et al, 1984). VmW65 does not attach directly to DNA (Marsden et al, 1987), but binds one or more host cellular factors (including Oct-l) to form a multiprotein complex IEC which interacts with TAATGARATTC (O'Hare et al, 1988;Preston et al, 1988). After interaction of the multiprotein complex with the cis-acting sequences upstream of the mRNA start site, the strongly acidic Cterminal 80 amino acids of VmW65 bind the transcription complex and enhance transcription Sadowski et al, 1988;Cousens et al, 1989).…”