Key result
Transmission electron microscopy revealed that the 2C protein from echovirus 30 forms hexameric ring-shaped particles with an external diameter of ~12 nm, resembling superfamily 3 DNA virus helicases.
The 2C protein of echovirus 30 forms hexameric ring-shaped structures similar to superfamily 3 DNA virus helicases, providing structural insight into this emerging antiviral target.
The 2C protein, which is an essential ATPase and one of the most conserved proteins across the Picornaviridae family, is an emerging antiviral target for which structural and functional characterization remain elusive. Based on a distant relationship to helicases of small DNA viruses, piconavirus 2C proteins have been predicted to unwind double-stranded RNAs. Here, a terminally extended variant of the 2C protein from echovirus 30 has been studied by means of enzymatic activity assays, transmission electron microscopy, atomic force microscopy and dynamic light scattering. The transmission electron-microscopy technique showed the existence of ring-shaped particles with ∼12 nm external diameter. Image analysis revealed that these particles were hexameric and resembled those formed by superfamily 3 DNA virus helicases.
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Papageorgiou et al. (2010) studied Echovirus 30 infection. 2C protein from echovirus 30 was evaluated on Structural characterization of the 2C protein. Transmission electron microscopy revealed that the 2C protein from echovirus 30 forms hexameric ring-shaped particles with an external diameter of ~12 nm, resembling superfamily 3 DNA virus helicases.
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