The proteins of five herpesviruses — herpes simplex types 1 and 2 (HSV-1 and HSV-2), bovine mammillitis virus (BMV), pseudorabies virus (PRV) and equine abortion virus (EAV) — have been compared by polyacrylamide gel electrophoresis of purified virus and by antigenic analysis using virus neutralization and agar-gel immunodiffusion tests. Although there were general similarities in the number, size range and overall complexity of polypeptides separated by polyacrylamide gel electrophoresis from purified particles of the five viruses, no single component of identical mobility was present in all viruses. The major capsid polypeptide from each of the five viruses comprised about 10% of virion protein mass but had distinctive mol. wt. of 158000 to 160000 (HSV-2 and BMV), 145000 (EAV) and 140000 (PRV) relative to 155000 for HSV-1.

Despite differences of apparent mol. wt. there was a one-for-one correspondence for the majority of structural polypeptides of HSV-1 and HSV-2 and many polypeptides of BMV were recognizably analogous to those of HSV-1 and HSV-2. In contrast the polypeptides of PRV and, more particularly, EAV differed markedly from those of all the other viruses. The antigenic analysis complemented these results; HSV-1, HSV-2 and BMV all cross-neutralized, whereas PRV and EAV were only neutralized by homologous antisera. Agar gel immunodiffusion tests with extracts of infected cells demonstrated at least one antigen common to all five viruses and showed BMV to be more closely related to HSV-1 and HSV-2 than were PRV or EAV although less closely related than HSV-1 to HSV-2. PRV and EAV share more antigens with each other than with the other viruses.


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