Structural insights into the assembly and regulation of distinct viral capsid complexes

Subir Sarker, María C. Terrón, Yogesh Khandokar, David Aragão, Joshua M. Hardy, Mazdak Radjainia, Manuel Jiménez-Zaragoza, Pedro J. de Pablo, Fasséli Coulibaly (), Daniel Luque, Shane R. Raidal () and Jade K. Forwood ()
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Subir Sarker: School of Animal and Veterinary Sciences, Charles Sturt University
María C. Terrón: Centro Nacional de Microbiología/ISCIII,
Yogesh Khandokar: School of Biomedical Sciences, Charles Sturt University
David Aragão: Australian Synchrotron
Joshua M. Hardy: Infection and Immunity Program, Monash University
Mazdak Radjainia: Infection and Immunity Program, Monash University
Manuel Jiménez-Zaragoza: Física de la Materia Condensada, Universidad Autónoma de Madrid
Pedro J. de Pablo: Física de la Materia Condensada, Universidad Autónoma de Madrid
Fasséli Coulibaly: Infection and Immunity Program, Monash University
Daniel Luque: Centro Nacional de Microbiología/ISCIII,
Shane R. Raidal: School of Animal and Veterinary Sciences, Charles Sturt University
Jade K. Forwood: Graham Centre for Agricultural Innovation

Nature Communications, 2016, vol. 7, issue 1, 1-7

Abstract: Abstract The assembly and regulation of viral capsid proteins into highly ordered macromolecular complexes is essential for viral replication. Here, we utilize crystal structures of the capsid protein from the smallest and simplest known viruses capable of autonomously replicating in animal cells, circoviruses, to establish structural and mechanistic insights into capsid morphogenesis and regulation. The beak and feather disease virus, like many circoviruses, encode only two genes: a capsid protein and a replication initiation protein. The capsid protein forms distinct macromolecular assemblies during replication and here we elucidate these structures at high resolution, showing that these complexes reverse the exposure of the N-terminal arginine rich domain responsible for DNA binding and nuclear localization. We show that assembly of these complexes is regulated by single-stranded DNA (ssDNA), and provide a structural basis of capsid assembly around single-stranded DNA, highlighting novel binding interfaces distinct from the highly positively charged N-terminal ARM domain.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13014

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DOI: 10.1038/ncomms13014

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