Structural basis for assembly of vertical single β-barrel viruses

Isaac Santos-Pérez, Diego Charro, David Gil-Carton, Mikel Azkargorta, Felix Elortza, Dennis H. Bamford, Hanna M. Oksanen and Nicola G. A. Abrescia ()
Additional contact information
Isaac Santos-Pérez: CIBERehd
Diego Charro: CIBERehd
David Gil-Carton: CIBERehd
Mikel Azkargorta: ProteoRed-ISCIII
Felix Elortza: ProteoRed-ISCIII
Dennis H. Bamford: University of Helsinki
Hanna M. Oksanen: University of Helsinki
Nicola G. A. Abrescia: CIBERehd

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: Abstract The vertical double β-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 Å 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 β-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 β-barrel MCPs.

Date: 2019
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DOI: 10.1038/s41467-019-08927-2

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