Download MendeleyLimits of Structural Plasticity in a Picornavirus Capsid Revealed by a Massively Expanded Equine Rhinitis a Virus Particle.
Bakker, S.E., Groppelli, E., Pearson, A.R., Stockley, P.G., Rowlands, D.J., Ranson, N.A.(2014) J Virol 88: 6093
- PubMed: 24648455
- DOI: https://doi.org/10.1128/JVI.01979-13
- Primary Citation of Related Structures:
4CTF, 4CTG - PubMed Abstract:
The Picornaviridae family of small, nonenveloped viruses includes major pathogens of humans and animals. They have positive-sense, single-stranded RNA genomes, and the mechanism(s) by which these genomes are introduced into cells to initiate infection remains poorly understood. The structures of presumed uncoating intermediate particles of several picornaviruses show limited expansion and some increased porosity compared to the mature virions. Here, we present the cryo-electron microscopy structure of native equine rhinitis A virus (ERAV), together with the structure of a massively expanded ERAV particle, each at ∼17-Å resolution. The expanded structure has large pores on the particle 3-fold axes and has lost the RNA genome and the capsid protein VP4. The expanded structure thus illustrates both the limits of structural plasticity in such capsids and a plausible route by which genomic RNA might exit.
Organizational Affiliation:
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.
