Preparation and Characterization of Monomodal Grapevine Virus A Capsid Protein

Protein Pept Lett. 2015;22(8):712-8. doi: 10.2174/0929866522666150625111607.

Abstract

Grapevine virus A (GVA), a flexible filament of approximately 800 nm in length is composed of capsid subunits that spontaneously assembles around a positive sense genomic RNA. In addition to encapsidation, plant viruses capsid proteins (CPs) participate in other processes throughout infection and GVA CP is involved in cell-to-cell translocation of the virus. A protocol was developed to obtain low-molecular weight GVA-CP that is not prone to aggregation and spontaneous assembly and this was characterized by circular dichroism and dynamic light scattering. These results indicate the suitably of GVA-CP for X-ray crystallographic and NMR studies that should lead to the elucidation of the first three-dimensional structure of a flexible filamentous virus from the Betaflexiviridae family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Capsid Proteins / chemistry*
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Dynamic Light Scattering
  • Flexiviridae / chemistry
  • Flexiviridae / genetics*
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism*
  • Sequence Alignment

Substances

  • Capsid Proteins
  • Recombinant Proteins