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The 4.4 A structure of the giant Melbournevirus virion belonging to the Marseilleviridae family

Burton-Smith, R. N.; Reddy, H. K. N.; Svenda, M.; Abergel, C.; Okamoto, K.; Murata, K.

2021-07-14 microbiology
10.1101/2021.07.14.452405 bioRxiv
Show abstract

Members of Marseilleviridae, one family of icosahedral giant viruses classified in 2012 have been identified worldwide in all types of environments. The virion shows a characteristic internal membrane extrusion at the five-fold vertices of the capsid, but its structural details need to be elucidated. We now report the 4.4 [A] cryo-electron microscopy structure of the Melbournevirus capsid. An atomic model of the major capsid protein (MCP) shows a unique cup structure on the trimer that accommodates additional proteins. A polyalanine model of the penton base protein shows internally extended N- and C-terminals, which indirectly connect to the internal membrane extrusion. The Marseilleviruses share the same orientational organisation of the MCPs as PBCV-1 and CroV, but do not appear to possess a protein akin to the "tape measure" of these viruses. Minor capsid proteins named PC-{beta}, zipper, and scaffold are proposed to control the dimensions of the capsid during assembly.

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