The product of the UL6 gene of herpes simplex virus type 1 is associated with virus capsids.

We report on the analysis of the UL6 and UL7 open reading frames of the herpes simplex virus type 1 (HSV-1) genome. The UL6 and UL7 transcripts were identified in HSV-1-infected cells by Northern blotting and shown to be coterminal at their 3' ends. Both transcripts were synthesized in the presence of phosphonoacetic acid, although in reduced amounts, indicating that UL6 and UL7 are expressed as delayed-early or gamma-1 genes. The 5' ends of the two transcripts were mapped by S1 nuclease and primer extension analysis. A polyclonal antiserum directed against an Escherichia coli-expressed 6 x His-UL6 fusion protein identified a protein of approximate M(r) 75,000 in cells infected with either HSV-1 or with a vaccinia virus recombinant expressing the HSV-1 UL6 protein. As with the transcript, the UL6 protein was synthesized at reduced levels in the absence of viral DNA replication. Western immunoblotting showed that the UL6 protein was present in purified virions but not in L-particles of HSV-1, and that it was located exclusively in the tegument/capsid fraction of virion. Further analysis of the UL6 protein revealed that this protein was associated with virus capsids.