Viral genome packaging machines: Structure and enzymology

Carlos E. Catalano, Marc C. Morais

Research output: Chapter in Book/Report/Conference proceedingChapter


Although the process of genome encapsidation is highly conserved in tailed bacteriophages and eukaryotic double-stranded DNA viruses, there are two distinct packaging pathways that these viruses use to catalyze ATP-driven translocation of the viral genome into a preassembled procapsid shell. One pathway is used by ϕ29-like phages and adenoviruses, which replicate and subsequently package a monomeric, unit-length genome covalently attached to a virus/phage-encoded protein at each 5′-end of the dsDNA genome. In a second, more ubiquitous packaging pathway characterized by phage lambda and the herpesviruses, the viral DNA is replicated as multigenome concatemers linked in a head-to-tail fashion. Genome packaging in these viruses thus requires excision of individual genomes from the concatemer that are then translocated into a preassembled procapsid. Hence, the ATPases that power packaging in these viruses also possess nuclease activities that cut the genome from the concatemer at the beginning and end of packaging. This review focuses on proposed mechanisms of genome packaging in the dsDNA viruses using unit-length ϕ29 and concatemeric λ genome packaging motors as representative model systems.

Original languageEnglish (US)
Title of host publicationViral Replication Enzymes and their Inhibitors Part B
EditorsCraig E. Cameron, Jamie J. Arnold, Laurie S. Kaguni
PublisherAcademic Press
Number of pages45
ISBN (Print)9780323900164
StatePublished - Jan 2021

Publication series

ISSN (Print)1874-6047


  • ASCE superfamily
  • ATPase
  • Biological motor enzymology
  • Molecular motors
  • Physical virology
  • Viral genome maturation
  • Viral genome packaging
  • Virus replication

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Biochemistry
  • Molecular Biology


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