Archives of Virology

, Volume 158, Issue 5, pp 933–942

Characterization and immunogenicity of norovirus capsid-derived virus-like particles purified by anion exchange chromatography

Original Article

DOI: 10.1007/s00705-012-1565-7

Cite this article as:
Huhti, L., Tamminen, K., Vesikari, T. et al. Arch Virol (2013) 158: 933. doi:10.1007/s00705-012-1565-7


Recombinant baculovirus (BV) expression systems are widely applied in the production of viral capsid proteins and virus-like particles (VLPs) for use as immunogens and vaccine candidates. Traditional density gradient purification of VLPs does not enable complete elimination of BV-derived impurities, including live viruses, envelope glycoprotein gp64 and baculoviral DNA. We used an additional purification system based on ionic strength to purify norovirus (NoV) GII-4 capsid-derived VLPs. The anion exchange chromatography purification led to highly purified VLPs free from BV impurities with intact morphology. In addition, highly purified VLPs induced strong NoV-specific antibody responses in BALB/c mice. Here, we describe a method for NoV VLP purification and several methods for determining their purity, including quantitative PCR for BV DNA detection.

Copyright information

© Springer-Verlag Wien 2012

Authors and Affiliations

  • L. Huhti
    • 1
  • K. Tamminen
    • 1
  • T. Vesikari
    • 1
  • V. Blazevic
    • 1
  1. 1.Vaccine Research CenterUniversity of Tampere Medical SchoolTampereFinland

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