4CTF

The limits of structural plasticity in a picornavirus capsid revealed by a massively expanded equine rhinitis A virus particle

This is a non-PDB format compatible entry.

Summary for 4CTF

• Entry DOI: 10.2210/pdb4ctf/pdb
• EMDB information: 2389
• Descriptor: VP1, EQUINE RHINITIS A VIRUS, P1, ... (4 entities in total)
• Functional Keywords: virus, picornavirus, capsid structure, capsid expansion, uncoating
• Biological source: EQUINE RHINITIS A VIRUS; More
• Total number of polymer chains: 240
• Total formula weight: 5102611.20

Authors

Bakker, S.E.,Groppelli, E.,Pearson, A.R.,Stockley, P.G.,Rowlands, D.J.,Ranson, N.A. (deposition date: 2014-03-13, release date: 2014-05-21, Last modification date: 2024-05-08)

Primary citation

Bakker, S.E.,Groppelli, E.,Pearson, A.R.,Stockley, P.G.,Rowlands, D.J.,Ranson, N.A.
Limits of Structural Plasticity in a Picornavirus Capsid Revealed by a Massively Expanded Equine Rhinitis a Virus Particle.
J.Virol., 88:6093-, 2014

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.

PubMed: 24648455
DOI: 10.1128/JVI.01979-13

Experimental method

ELECTRON MICROSCOPY (17 Å)