Herpesvirus assembly: An update

The order Herpesvirales contains viruses infecting animals from molluscs to men with a common virion morphology which have been classified into the families Herpesviridae, Alloherpesviridae and Malacoherpesviridae. Herpes virions are among the most complex virus particles containing a multitude of viral and cellular proteins which assemble into nucleocapsid, envelope and tegument. After autocatalytic assembly of the capsid and packaging of the newly replicated viral genome, a process which occurs in the nucleus and resembles head formation and genome packaging in the tailed double-stranded DNA bacteriophages, the nucleocapsid is translocated to the cytoplasm by budding at the inner nuclear membrane followed by fusion of the primary envelope with the outer nuclear membrane. Viral and cellular proteins are involved in mediating this ‘nuclear egress’ which entails substantial remodeling of the nuclear architecture. For final maturation within the cytoplasm tegument components associate with the translocated nucleocapsid, with themselves, and with the future envelope containing viral membrane proteins in a complex network of interactions resulting in the formation of an infectious herpes virion. The diverse interactions between the involved proteins exhibit a striking redundancy which is still insufficiently understood. In this review, recent advances in our understanding of the molecular processes resulting in herpes virion maturation will be presented and discussed as an update of a previous contribution [Mettenleiter, T.C., 2004. Budding events in herpesvirus morphogenesis. Virus Res. 106, 167–180].