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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
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