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Assembly of Simple Icosahedral Viruses

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Structure and Physics of Viruses

Part of the book series: Subcellular Biochemistry ((SCBI,volume 68))

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 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.

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Abbreviations

AAP:

assembly-activating protein

AAV:

adeno-associated virus

CBB:

capsid building block

CP:

capsid protein

CPV:

canine parvovirus

DBD:

DNA-binding domains

H1-PV:

parvovirus H1

hr-t:

host range-transforming

FPV:

feline parvovirus

MEV:

mink enteritis virus

MVM:

minute virus of mice

NLM:

nuclear localization motif

NLS:

nuclear localization sequence

NPC:

nuclear pore complex

PPV:

porcine parvovirus

SV40:

simian virus 40

VLP:

virus-like particle

VP:

viral protein

5x:

five-fold axis

3x:

three-fold axis

2x:

two-fold axis.

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Acknowledgements

I gratefully acknowledge the collaborative work of Mavis Agbandje-Mckenna (University of Florida) on solving parvovirus MVMp capsid structure to atomic resolution, of Mauricio G. Mateu (CBMSO, Universidad Autónoma de Madrid) on MVM assembly, and of Thomas L. Benjamin (Harvard Medical School, Massachussets) on aspects related to Polyomavirus assembly. The many inspiring conversations along the years with regular participants to the “Virus Assembly” FASEB meeting (Vermont Academy, USA), in particular with Peter Tattersall (Yale University, Connecticut), are also deeply acknowledged. This review stands from the experience gained by the author on Parvovirus assembly thanks to the enthusiastic work of Eva Hernando, Eleuterio Lombardo, Beatriz Maroto, Juan C. Ramírez, Laura Riolobos, and Noelia Valle. Support on figures design by Jon Gil-Ranedo and Jorge Sánchez is also acknowledged. Research in JM Almendral’s laboratory is currently supported by grant SAF 2011-29403 from the Spanish Ministerio de Ciencia e Innovación.

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Authors and Affiliations

  1. Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM) and Department of Molecular Biology, Universidad Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain

    José M. Almendral

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  1. José M. Almendral
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Correspondence to José M. Almendral .

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  1. "Severo Ochoa" (CSIC_UAM), And Dept. of Molecular Biology, Centro de Biología Molecular, Cantoblanco, Madrid, 28049, Madrid, Spain

    Mauricio G. Mateu

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Almendral, J.M. (2013). Assembly of Simple Icosahedral Viruses. In: Mateu, M. (eds) Structure and Physics of Viruses. Subcellular Biochemistry, vol 68. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6552-8_10

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