in vitro interaction of hsv-1 orf p with both thymidine kinase (tk) and an unidentified cellular protein

herpes simplex virus type-1 (hsv-1) is a neurotropic pathogen of humans that establishes latent infection in the sensory ganglia innervating the site of primary infection. a number of genes control hsv-1 pathogenicity and latency. open reading frame p (orf p) is one of these genes that might have a role in latency and pathogenesis. a complication in the analysis of the role of orf p in the hsv-1 life-cycle is an antisense overlapping gene, icp34.5. orf p is also deleted in icp34.5 negative mutants and to date, no definite function is attributed to it. an approach to analyze the function of a viral gene such as orf p is to determine if this gene interacts with any of the cellular and viral proteins both in vitro and in vivo. therefore, in this work, using gst pulldown assay and western-blotting, it was investigated that with which cellular and viral gene products orf p interacts. our results showed that orf p interacted with thymidine kinase (tk) and also with an unidentified cellular protein. conclusively the results of these works to-gether suggest possible role for orf p in both splicing and replication of hsv-1.