Antigenic and Structural Conservation of Herpesvirus DNA-binding Proteins

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Abstract
A common antigen of several herpesviruses (pseudorabies virus, equine abortion virus and bovine mammillitis virus) was previously shown to be antigenically related to the major DNA-binding proteins of herpes simplex virus types 1 and 2. The cross-reacting polypeptide from cells [hamster kidney BHK-21 and human laryngeal carcinoma HEp-2] infected with pseudorabies virus, equine abortion virus and bovine mammillitis virus were purified and the cross-reacting protein was shown to be a major DNA-binding protein for each virus. Tryptic peptide analysis of the cross-reacting DNA-binding proteins of all 5 viruses has shown structural similarities. The proteins thus were shown to share common antigenic sites, to have similar biological properties and to have a highly conserved amino acid sequence. This unexpected similarity between proteins from diverse herpesviruses suggests an essential and fundamental role of the major DNA-binding protein in herpesvirus replication.