Abstract
The major herpes simplex virus type 2 DNA-binding infected cell-specific polypeptides 11 and 12 have been purified to homogeneity from extracts of virus-infected cells. Monospecific antiserum to the purified protein has been made and used to examine virus temperature-sensitive mutants for defects in the synthesis of the protein and to probe virus DNA synthesis in isolated chromatin. The purified protein acted directly on a polydeoxyadenylic acid-polydeoxythymidylic acid helix, reducing its melting temperature. The results indicated that the protein functions in virus DNA synthesis.