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Título

Assembly of simple icosahedral viruses

AutorAlmendral, José M.
Palabras claveMaturation cleavage
Virus factory
Encapsidation
Packaging
Nucleation
Icosahedral capsid
Triangulation number
Assembly intermediate
Protein contacts
Nuclear translocation
Protein folding
Fecha de publicación2013
EditorPlenum Press
CitaciónSub-Cellular Biochemistry 68: 307- 328 (2013)
ResumenIcosahedral 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 hydrophobic contacts and non-covalent interactions in assembly intermediates, which serve as blocks to build a symmetric capsid. In some cases, non-symmetric interactions among intermediates are involved in assembly, highlighting the remarkable capacity of capsid proteins to fold into demanding conformations compatible with a closed protein shell. In this chapter, the morphogenesis of structurally simple icosahedral viruses, including representative members of the parvoviruses, picornaviruses or polyomaviruses as paradigms, is described in some detail. Icosahedral virus assembly may occur in different subcellular compartments and involve a panoplia of cellular and viral factors, chaperones, and protein modifications that, in general, are still poorly characterized. Mechanisms of viral genome encapsidation may imply direct interactions between the genome and the assembly intermediates, or active packaging into a preformed empty capsid. High stability of intermediates and proteolytic cleavages during viral maturation usually contribute to the overall irreversible character of the assembly process. These and other simple 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 viruses and cellular and synthetic macromolecular complexes.
URIhttp://hdl.handle.net/10261/117126
DOI10.1007/978-94-007-6552-8_10
Identificadoresdoi: 10.1007/978-94-007-6552-8_10
issn: 0306-0225
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