Production of Norovirus VLPs to size homogeneity

Virus Res. 2015 Jun 2:204:1-5. doi: 10.1016/j.virusres.2015.04.009. Epub 2015 Apr 17.

Abstract

Expression of full-length major capsid protein of Noroviruses (NoVs) in sf9 cells using recombinant baculovirus expression system leads to the formation of virus-like particles (VLPs) with two sizes. In our pursuit of VLPs with uniform sizes, we find that N terminal truncated capsid protein formed primary VLPs with an average size of 21 nm. This kind of VLPs showed similar binding patterns to those produced with full-length major capsid protein. HBGA-VLPs binding assay and saliva-VLPs blocking analysis, as well as stability test demonstrate that the smaller 21 nm VLPs might be an excellent candidate for NoVs vaccine.

Keywords: Norovirus; Smaller viral particles; Truncated capsid protein; VLPs.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caliciviridae Infections / virology
  • Capsid / ultrastructure
  • Capsid Proteins / genetics*
  • Capsid Proteins / metabolism
  • Gene Expression
  • Molecular Sequence Data
  • Norovirus / genetics
  • Norovirus / ultrastructure*
  • Particle Size
  • Sequence Alignment
  • Sequence Deletion
  • Sf9 Cells
  • Spodoptera

Substances

  • Capsid Proteins