Antigenic and Structural Conservation of Herpesvirus DNA-binding Proteins

• Published in: Journal of general virology Vol. 56; no. 2; pp. 409 - 419
• Main Authors: Littler, Edward, Yeo, Jane, Killington, R. A, Purifoy, Dorothy J. M, Powell, Kenneth L
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01.10.1981
• Subjects: Amino Acid Sequence; antigenic characteristics; Carrier Proteins - analysis; Carrier Proteins - immunology; Cross Reactions; DNA-binding protein; DNA-Binding Proteins; Epitopes; Herpesviridae - analysis; Herpesviridae - immunology; herpesvirus; Herpesvirus 1, Equid - analysis; Herpesvirus 1, Suid - analysis; isolation; Peptides - analysis; Simplexvirus - analysis; Viral Proteins - analysis; Viral Proteins - immunology
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-56-2-409

Department of Microbiology, University of Leeds, Leeds LS2 9JT, U.K. 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 herpesviruses suggests an essential and fundamental role of the major DNA-binding protein in herpes virus replication. Keywords: herpesvirus, DNA-binding proteins, common antigen Received 26 February 1981; accepted 10 June 1981.