Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions.
Herpesviruses, a family of animal viruses with large (125-250 kbp) linear DNA genomes, are highly diversified in terms of host range; nevertheless, their virions conform to a common architecture. The genome is confined at high density within a thick-walled icosahedral capsid with the uncommon (among viruses, generally) but unvarying triangulation number T = 16. The envelope is a membrane in which some 11 different viral glycoproteins are implanted. Between the capsid and the envelope is a capacious compartment called the tegument that accommodates ∼20-40 different viral proteins (depending on which virus) destined for delivery into a host cell. A strong body of evidence supports the hypothesis that herpesvirus capsids and those of tailed bacteriophages stem from a distant common ancestor, whereas their radically different infection apparatuses - envelope on one hand and tail on the other - reflect subsequent coevolution with divergent hosts. Here we review the molecular components of herpesvirus capsids and the mechanisms that regulate their assembly, with particular reference to the archetypal alphaherpesvirus, herpes simplex virus type 1; assess their duality with the capsids of tailed bacteriophages; and discuss the mechanism whereby, once DNA packaging has been completed, herpesvirus nucleocapsids exit from the nucleus to embark on later stages of the replication cycle.
National Institute for Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Giovanni
G
Cardone
J Bernard
JB
Heymann
Naiqian
N
Cheng
Benes L
BL
Trus
Alasdair C
AC
Steven
D000818:Animals; D002213:Capsid / Q000378:metabolism* / Q000648:ultrastructure; D006564:Herpesviridae / Q000378:metabolism* / Q000472:pathogenicity / Q000648:ultrastructure*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D014771:Virion / Q000378:metabolism* / Q000648:ultrastructure; D019065:Virus Assembly; D014779:Virus Replication
D014764:Viral Proteins