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2016-Sarker et al-NatCcomms13014-Structural insights into the assembly and regulation of distinct viral capsid complexes.pdf (1.52 MB)

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

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posted on 09.11.2020, 00:25 by S Sarker, MC Terron, Y Khandokar, D Aragao, JM Hardy, M Radjainia, M Jimenez-Zaragoza, PJ de Pablo, F Coulibaly, D Luque, SR Raidal, JK Forwood
© The Author(s) 2016. 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.

Funding

J.K.F. and F.C. are funded by Future Fellowships of the Australian Research Council. We thank the Clive and Vera Ramaciotti Centre for Cryo Electron Microscopy and the Australian Synchrotron for their technical support.

Australian Research Council

History

Publication Date

01/01/2016

Journal

Nature Communications

Volume

7

Issue

1

Article Number

13014

Pagination

7p.

Publisher

Nature Publishing Group

ISSN

2041-1723

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The Authors reserves all moral rights over the deposited text and must be credited if any re-use occurs. Documents deposited in OPAL are the Open Access versions of outputs published elsewhere.

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