Assembly of complex viruses exemplified by a halophilic euryarchaeal virus

Show full item record



Permalink

http://hdl.handle.net/10138/301539

Citation

De Colibus , L , Roine , E , Walter , T S , Ilca , S L , Wang , X , Wang , N , Roseman , A M , Bamford , D , Huiskonen , J T & Stuart , D 2019 , ' Assembly of complex viruses exemplified by a halophilic euryarchaeal virus ' , Nature Communications , vol. 10 , 1456 . https://doi.org/10.1038/s41467-019-09451-z

Title: Assembly of complex viruses exemplified by a halophilic euryarchaeal virus
Author: De Colibus, Luigi; Roine, Elina; Walter, Thomas S.; Ilca, Serban L.; Wang, Xiangxi; Wang, Nan; Roseman, Alan M.; Bamford, Dennis; Huiskonen, Juha T.; Stuart, David
Contributor: University of Helsinki, Helsinki Institute of Sustainability Science (HELSUS)
University of Helsinki, Biosciences
University of Helsinki, Helsinki Institute of Life Science HiLIFE
Date: 2019-03-29
Language: eng
Number of pages: 9
Belongs to series: Nature Communications
ISSN: 2041-1723
URI: http://hdl.handle.net/10138/301539
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.
Subject: CRYO-EM
CRYOELECTRON MICROSCOPY
STRUCTURES REVEAL
VALIDATION
REFINEMENT
PROTEIN
MODEL
SH1
DEFOCUS
SYSTEM
1183 Plant biology, microbiology, virology
Rights:


Files in this item

Total number of downloads: Loading...

Files Size Format View
s41467_019_09451_z.pdf 2.585Mb PDF View/Open

This item appears in the following Collection(s)

Show full item record