Antigenic and structural conservation of herpesvirus DNA-binding proteins.
Previously, we have shown a common antigen of several herpesviruses (pseudorabies virus, equine abortion virus and bovine mammillitis virus) to be antigenically related to the major DNA-binding proteins of herpes simplex virus types 1 and 2. In this study we have purified the cross-reacting polypeptide from cells infected with pseudorabies virus, equine abortion virus and bovine mammillitis virus and shown the cross-reacting protein to be a major DNA-binding protein for each virus. Tryptic peptide analysis of the cross-reacting DNA-binding proteins of all five 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 herpes viruses suggests an essential and fundamental role of the major DNA-binding protein in herpes virus replication.
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000032:analysis* / Q000276:immunology; D003429:Cross Reactions; D004268:DNA-Binding Proteins; D000939:Epitopes; D006564:Herpesviridae / Q000032:analysis* / Q000276:immunology; D004861:Herpesvirus 1, Equid / Q000032:analysis; D011558:Herpesvirus 1, Suid / Q000032:analysis; D010455:Peptides / Q000032:analysis; D018139:Simplexvirus / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis* / Q000276:immunology
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D000939:Epitopes; D010455:Peptides; D014764:Viral Proteins