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

Subject Areas: Biology and Bio-materials


Technical Areas:

Documents:
s41467-019-09451-z.pdf