Cypovirus capsid protein VP5 has nucleoside triphosphatase activity
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As a major protein of cypovirus capsid shell, VP5 performs as the clamp protein to stabilize the capsid shell structure (Yu et al., 2008). And as a part of viral RNA (vRNA) replication machinery, VP5 has been found to possess an ATP-independent RNA chaperoning activity (Yang et al., 2014). Here, we report that VP5 also has the nucleoside triphosphatase (NTPase) activity, which can hydrolyze all kinds of NTPs and dNTPs. Thus, our finding reveals that VP5 is a multifunctional protein that may be involved in diverse processes during cypoviral life cycle.
The family Reoviridae is a large group of double-stranded RNA (dsRNA) viruses that include numerous important human and animal pathogens responsible for diseases in humans, livestock animals, insects and plants (Mertens, 2004). And the typical characteristic of dsRNA viruses is that their viral inner capsids are the machineries for vRNA replication. Reoviruses contain a layer of inner capsid shell and one or two outer layers...