2026-06-14T05:06:34Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/92672024-09-27T23:09:24Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Sarker, Subir author Terrón-Orellana, Maria Carmen author Khandokar, Yogesh author Aragão, David author Hardy, Joshua M author Radjainia, Mazdak author Jiménez-Zaragoza, Manuel author de Pablo, Pedro J author Coulibaly, Fasséli author Luque, Daniel author Raidal, Shane R author Forwood, Jade K author 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. Nat Commun. 2016 Oct 4;7:13014. 10.1038/ncomms13014 2041-1723 2041-1723 Nature communications 27698405 http://hdl.handle.net/20.500.12105/9267 Structural insights into the assembly and regulation of distinct viral capsid complexes