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Assembly of complex viruses exemplified by a halophilic euryarchaeal virus
DOI:
10.1038/s41467-019-09451-z
Authors:
Luigi
De Colibus
(Wellcome Centre for Human Genetics, University of Oxford)
,
Elina
Roine
(University of Helsinki)
,
Thomas S.
Walter
(Wellcome Centre for Human Genetics, University of Oxford)
,
Serban L.
Ilca
(Wellcome Centre for Human Genetics, University of Oxford)
,
Xiangxi
Wang
(Institute of Biophysics, Chinese Academy of Sciences)
,
Nan
Wang
(Institute of Biophysics, Chinese Academy of Sciences)
,
Alan M.
Roseman
(University of Manchester)
,
Dennis
Bamford
(University of Helsinki)
,
Juha T.
Huiskonen
(Wellcome Centre for Human Genetics, University of Oxford; University of Helsinki)
,
David I.
Stuart
(Wellcome Centre for Human Genetics, University of Oxford; Diamond Light Source)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Nature Communications
, VOL 10
State:
Published (Approved)
Published:
March 2019

Abstract: Many of the largest known viruses belong to the PRD1-adeno structural lineage characterised by conserved pseudo-hexameric capsomers composed of three copies of a single major capsid protein (MCP). Here, by high-resolution cryo-EM analysis, we show that a class of archaeal viruses possess hetero-hexameric MCPs which mimic the PRD1-adeno lineage trimer. These hetero-hexamers are built from heterodimers and utilise a jigsaw-puzzle system of pegs and holes, and underlying minor capsid proteins, to assemble the capsid laterally from the 5-fold vertices. At these vertices proteins engage inwards with the internal membrane vesicle whilst 2-fold symmetric horn-like structures protrude outwards. The horns are assembled from repeated globular domains attached to a central spine, presumably facilitating multimeric attachment to the cell receptor. Such viruses may represent precursors of the main PRD1-adeno lineage, similarly engaging cell-receptors via 5-fold spikes and using minor proteins to define particle size.
Journal Keywords: Cryoelectron microscopy; Viral evolution; Virus structures
Diamond Keywords: Viruses
Subject Areas:
Biology and Bio-materials
Technical Areas:
Added On:
04/04/2019 09:47
Documents:
s41467-019-09451-z.pdf
Discipline Tags:
Pathogens
Infectious Diseases
Health & Wellbeing
Structural biology
Life Sciences & Biotech
Technical Tags: