Key result
14S pentameric particles and mature virions displayed nonspecific RNA-binding activity and formed rapidly sedimenting complexes, whereas 75S empty capsids showed no propensity to associate with RNA.
14S pentameric particles of poliovirus display RNA-binding activity and undergo conformational changes, suggesting a direct role in RNA packaging during viral morphogenesis.
Differentiates RNA affinity among assembly intermediates; leaves open roles in replication cycles.
The mechanism of encapsidation of the RNA genome of poliovirus and other picornaviruses is unknown. To test whether any of the putative assembly intermediates of poliovirus could interact directly with the poliovirus RNA genome, poliovirus RNA was attached to magnetic streptavidin beads and incubated with partially purified extracts containing 35S-labeled 14S pentamer and 75S empty-capsid subviral particles from infected cells. The amount of labeled protein bound to the beads was monitored, thus testing the RNA-binding activities of only the labeled viral proteins in the preparations. In this assay, nonspecific RNA-binding activity was displayed by the 14S pentameric particles and mature virons. 75S empty capsids displayed no propensity to associate with RNA. 14S pentamers were demonstrated to form rapidly sedimenting complexes and to undergo a conformational alteration upon RNA binding. These findings are consistent with a direct role for the 14S pentameric particles in RNA packaging during poliovirus morphogenesis.
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Nugent et al. (1995) studied Poliovirus infection. 14S pentamer and 75S empty-capsid subviral particles was evaluated on RNA-binding activity. 14S pentameric particles and mature virions displayed nonspecific RNA-binding activity and formed rapidly sedimenting complexes, whereas 75S empty capsids showed no propensity to associate with RNA.
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