Structural basis for assembly of vertical single β-barrel viruses

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Santos-Perez , I , Charro , D , Gil-Carton , D , Azkargorta , M , Elortza , F , Bamford , D H , Oksanen , H M & Abrescia , N G A 2019 , ' Structural basis for assembly of vertical single β-barrel viruses ' , Nature Communications , vol. 10 , 1184 . https://doi.org/10.1038/s41467-019-08927-2

Title: Structural basis for assembly of vertical single β-barrel viruses
Author: Santos-Perez, Isaac; Charro, Diego; Gil-Carton, David; Azkargorta, Mikel; Elortza, Felix; Bamford, Dennis H.; Oksanen, Hanna M.; Abrescia, Nicola G. A.
Contributor organization: Structure of the Viral Universe
Molecular and Integrative Biosciences Research Programme
Molecular Principles of Viruses
Aerovirology Research Group
Date: 2019-03-12
Language: eng
Number of pages: 9
Belongs to series: Nature Communications
ISSN: 2041-1723
DOI: https://doi.org/10.1038/s41467-019-08927-2
URI: http://hdl.handle.net/10138/301012
Abstract: The vertical double beta-barrel major capsid protein (MCP) fold, fingerprint of the PRD1-adeno viral lineage, is widespread in many viruses infecting organisms across the three domains of life. The discovery of PRD1-like viruses with two MCPs challenged the known assembly principles. Here, we present the cryo-electron microscopy (cryo-EM) structures of the archaeal, halophilic, internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) and Haloarcula hispanica icosahedral virus 2 (HHIV-2) at 3.7 and 3.8 angstrom resolution, respectively. Our structures reveal proteins located beneath the morphologically distinct two- and three-tower capsomers and homopentameric membrane proteins at the vertices that orchestrate the positioning of pre-formed vertical single beta-barrel MCP heterodimers. The cryo-EM based structures together with the proteomics data provide insights into the assembly mechanism of this type of viruses and into those with membrane-less double beta-barrel MCPs.
Subject: BACTERIOPHAGE PRD1
CAPSID PROTEIN
EVOLUTION
INSIGHTS
SH1
DNA
DISSOCIATION
REVEAL
MODEL
1183 Plant biology, microbiology, virology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion


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