Assembly of Structurally Simple Icosahedral Viruses

Alberto López-Bueno, Jon Gil-Ranedo, José M. Almendral*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Icosahedral viruses exhibit elegant pathways of capsid assembly and maturation regulated by symmetry principles. Assembly is a dynamic process driven by consecutive and genetically programmed morphogenetic interactions between protein subunits. The non-symmetric capsid subunits are gathered by non-covalent contacts and interactions in assembly intermediates, which serve as blocks to build a symmetric capsid. In some virus examples, the assembly of the protein shell further requires non-symmetric interactions among intermediates to fold into specific conformations. In this chapter, the morphogenesis of some small and structurally simple icosahedral viruses, including representative members of the parvoviruses, picornaviruses, and polyomaviruses as paradigms, is described in some detail. Despite their small size, the assembly of these icosahedral viruses may follow rather complex pathways, as they may occur in different subcellular compartments, involve a panoply of cellular and viral factors, and regulatory protein post-translational modifications that challenge its comprehensive understanding. Mechanisms of viral genome encapsidation may imply direct interactions between the genome and the assembly intermediates, or active packaging into a preformed empty capsid. Further, membranes and factors at specific subcellular compartments may also be critically required for virus maturation. The high stability of intermediates and the process of viral maturation contribute to the overall irreversible character of the assembly process. These and other small, structurally less complex icosahedral viruses were pioneer models to understand basic principles of virus assembly, continue to be leading subjects of morphogenetic analyses, and have inspired ongoing studies on the assembly of larger, structurally more complex viruses as well as cellular and synthetic macromolecular complexes.

Original languageEnglish
Title of host publicationSubcellular Biochemistry
PublisherSpringer Science and Business Media B.V.
Pages403-430
Number of pages28
DOIs
Publication statusPublished - 2024

Publication series

NameSubcellular Biochemistry
Volume105
ISSN (Print)0306-0225

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology
  • Cancer Research

Keywords

  • Assembly intermediate
  • Genome encapsidation
  • Icosahedral capsid
  • Maturation cleavage
  • Nuclear translocation
  • Nucleation
  • Protein folding
  • Protein phosphorylation
  • Protein–protein interactions
  • Triangulation number
  • Virus factory

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