Norovirus-binding proteins recovered from activated sludge micro-organisms with an affinity to a noroviral capsid peptide

J Appl Microbiol. 2010 Dec;109(6):1923-8. doi: 10.1111/j.1365-2672.2010.04821.x.

Abstract

Aims: Transmission routes of noroviruses, leading aetiological agents of acute gastroenteritis, are rarely verified when outbreaks occur. Because the destination of norovirus particles being firmly captured by micro-organisms could be totally different from that of those particles moving freely, micro-organisms with natural affinity ligands such as virus-binding proteins would affect the fate of viruses in environment, if such microbial affinity ligands exist. The aim of this study is to identify norovirus-binding proteins (NoVBPs) that are presumably working as natural ligands for norovirus particles in water environments.

Methods and results: NoVBPs were recovered from activated sludge micro-organisms by an affinity chromatography technique in which a capsid peptide of norovirus genogroup II (GII) was immobilized. The recovered NoVBPs bind to norovirus-like particles (NoVLPs) of norovirus GII, and this adsorption was stronger than that to NoVLPs of norovirus genogroup I. The profile of two-dimensional electrophoresis of NoVBPs showed that the recovered NoVBPs included at least seven spots of protein. The determination of N-terminal amino acid sequences of these NoVBPs revealed that hydrophobic interactions could contribute to the adsorption between NoVBPs and norovirus particles.

Conclusions: NoVBPs conferring a high affinity to norovirus GII were successfully isolated from activated sludge micro-organisms.

Significance and impact of the study: NoVBPs could be natural viral ligands and play an important role in the NoV transmission.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / metabolism*
  • Capsid Proteins / isolation & purification*
  • Capsid Proteins / metabolism
  • Chromatography, Affinity
  • Electrophoresis, Gel, Two-Dimensional
  • Hydrophobic and Hydrophilic Interactions
  • Immobilized Proteins / metabolism
  • Ligands
  • Molecular Sequence Data
  • Norovirus / metabolism*
  • Protein Binding
  • Sequence Analysis, Protein
  • Sewage / microbiology*
  • Sewage / virology

Substances

  • Bacterial Proteins
  • Capsid Proteins
  • Immobilized Proteins
  • Ligands
  • Sewage