Capsid protein structure, self-assembly, and processing reveal morphogenesis of the marine virophage mavirus.

ABSTRACT: Virophages have the unique property of parasitizing giant viruses within unicellular hosts. Little is understood about how they form infectious virions in this tripartite interplay. We provide mechanistic insights into assembly and maturation of mavirus, a marine virophage, by combining structural and stability studies on capsomers, virus-like particles (VLPs), and native virions. We found that the mavirus protease processes the double jelly-roll (DJR) major capsid protein (MCP) at multiple C-terminal sites and that these sites are conserved among virophages. Mavirus MCP assembled in Escherichia coli in the absence and presence of penton protein, forming VLPs with defined size and shape. While quantifying VLPs in E. coli lysates, we found that full-length rather than processe

SUBMITTER: Born D 

PROVIDER: S-EPMC6048507 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature