Abstract
The brevidensovirus is one of the smallest viruses in the world and the capsid of Aedes albopictus C6/36 cell densovirus (C6/36DNV) is the simplest and most compact capsid in brevidensovirus. To understand the assembly mechanism of icosahedral-virus capsid from this simplest model, we tried to express various lengths of virus proteins (VPs) of C6/36DNV in Bac-to-Bac ® system and evaluate their self-assembly capacities in insect Spodoptera frugiperda 9 (Sf9) cells. The result showed that the N-terminal GGSG sequence (residue 23–26), highly conserved glycine-rich region in Parvoviridae, and C-terminal GTGGVVTCMP (residue 344–353) were essential for capsid assembly, while the N-terminal nuclear localization signal, GTKRKR sequence (residue 15–20), was nonessential for the virus-like particles (VLPs) assembly, but did effect the formation of crystalline arrays in infected Sf9 cells. These information provided clues for how icosahedral-virus capsids formed and showed the potential of C6/36DNV-VLPs becoming a powerful nanoparticle vector.
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