Structural highlights
Publication Abstract from PubMed
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.
Assembly of complex viruses exemplified by a halophilic euryarchaeal virus.,Colibus L, Roine E, Walter TS, Ilca SL, Wang X, Wang N, Roseman AM, Bamford D, Huiskonen JT, Stuart DI Nat Commun. 2019 Mar 29;10(1):1456. doi: 10.1038/s41467-019-09451-z. PMID:30926810[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Colibus L, Roine E, Walter TS, Ilca SL, Wang X, Wang N, Roseman AM, Bamford D, Huiskonen JT, Stuart DI. Assembly of complex viruses exemplified by a halophilic euryarchaeal virus. Nat Commun. 2019 Mar 29;10(1):1456. doi: 10.1038/s41467-019-09451-z. PMID:30926810 doi:http://dx.doi.org/10.1038/s41467-019-09451-z