Further Characterization of the UL37 Protein of Herpes Simplex Virus Type 1 and its Interaction with ICP8, the Major DNA-Binding Protein of Herpes Simplex Virus
Uniformed Services University Of The Health Sciences Bethesda United States
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The UL37 protein of herpes simplex virus type 1 has been a focus of study in our laboratory. Previous studies demonstrated that the UL37 open reading frameORF encoded a 120 kDa protein which belonged to the gamma 1 class of HSV-1 genes in HSV-1-infected cells. In addition, the UL37 protein was found to co-elute from both single-stranded sS and double-stranded ds DNA columns with IPC8, the major DNA-binding protein of HSV-1. Comparative studies using a vaccinia virus recombinant, V37, and an ICP8 mutant, d21, strongly suggested that the apparent DNA binding exhibited by the UL37 protein from HSV-1-infected cells was due to an association with the ICP8 protein on these columns and not from an intrinsic affinity of the protein for DNA. The UL37 gene product was also classified as a nonstructural protein since it did not appear to be a component of the virion within the limits of detection.