Structural basis for assembly of vertical single β-barrel viruses

DOI: 10.1038/s41467-019-08927-2

Authors: Isaac Santos-perez (CIC bioGUNE) , Diego Charro (CIC bioGUNE) , David Gil-carton (CIC bioGUNE) , Mikel Azkargorta (CIC bioGUNE) , Felix Elortza (CIC bioGUNE) , Dennis H. Bamford (University of Helsinki) , Hanna M. Oksanen (University of Helsinki) , Nicola G. A. Abrescia (CIC bioGUNE; IKERBASQUE, Basque Foundation for Science)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: March 2019
Diamond Proposal Number(s): 17171

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.

Journal Keywords: Cryoelectron microscopy; Virus structures

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond

Documents:
s41467-019-08927-2.pdf