Gómez-Blanco J, Luque D, González JM, Carrascosa JL, Alfonso C, Trus B, Havens WM, Ghabrial SA, Castón JR.
Cryo-electron microscopy reconstruction of Cryphonectria nitschkei
virus 1, a dsRNA virus, shows that the capsid protein (60
copies/particle) is formed by a repeated helical core, indicative
of gene duplication. This unusual organization is
common to chrysoviruses.
The arrangement of many of these putative
α-helices
is conserved in the totivirus L-A capsid protein,
suggesting a shared motif. Our results indicate that a 120-subunit T=1
capsid
is a conserved architecture that optimizes dsRNA
replication and organization.