Apple latent spherical virus structure with stable capsid frame supports quasi-stable protrusions expediting genome release

Commun Biol. 2020 Sep 4;3(1):488. doi: 10.1038/s42003-020-01217-4.

Abstract

Picorna-like plant viruses are non-enveloped RNA spherical viruses of ~30 nm. Part of the survival of these viruses depends on their capsid being stable enough to harbour the viral genome and yet malleable enough to allow its release. However, molecular mechanisms remain obscure. Here, we report a structure of a picorna-like plant virus, apple latent spherical virus, at 2.87 Å resolution by single-particle cryo-electron microscopy (cryo-EM) with a cold-field emission beam. The cryo-EM map reveals a unique structure composed of three capsid proteins Vp25, Vp20, and Vp24. Strikingly Vp25 has a long N-terminal extension, which substantially stabilises the capsid frame of Vp25 and Vp20 subunits. Cryo-EM images also resolve RNA genome leaking from a pentameric protrusion of Vp24 subunits. The structures and observations suggest that genome release occurs through occasional opening of the Vp24 subunits, possibly suppressed to a low frequency by the rigid frame of the other subunits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid / metabolism*
  • Capsid / ultrastructure
  • Chenopodium / virology
  • Cryoelectron Microscopy
  • Genome, Viral*
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Subunits / metabolism
  • Secoviridae / chemistry*
  • Secoviridae / genetics*
  • Secoviridae / ultrastructure

Substances

  • Protein Subunits

Supplementary concepts

  • Apple latent spherical virus