Assembly of complex viruses exemplified by a halophilic euryarchaeal virus

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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 .

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 organization: Helsinki Institute of Sustainability Science (HELSUS)
University Management
Elina Roine / Principal Investigator
General Microbiology
Molecular and Integrative Biosciences Research Programme
Structure of the Viral Universe
Helsinki Institute of Life Science HiLIFE
Laboratory of Structural Biology
Aerovirology Research Group
Date: 2019-03-29
Language: eng
Number of pages: 9
Belongs to series: Nature Communications
ISSN: 2041-1723
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
1183 Plant biology, microbiology, virology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion

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