活性汚泥細菌から分離されたノロウイルス吸着タンパク質 (Norovirus-Binding Proteins : NoVBPs) の特性評価

概要

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In this study, norovirus-binding proteins (NoVBPs) were newly recovered from activated sludge culture using affinity chromatography. The C-terminal amino acid sequence (12 residues) of the Lordsdale virus, belonging to the dominant genotype (GII.4) of noroviruses throughout the world, was used as a ligand in the affinity chromatography. Two-dimensional electrophoresis analysis shows that the samples recovered by the affinity chromatography include a variety of proteins, which have a molecular weights between 60 and 10 kDa and isoelectric points between 3 and 6. The binding affinity of NoVBPs to the virus-like particle (VLP) of norovirus GII.4 was higher than that to the VLP of norovirus GI.1, which was indicated by ELISA. A determination of the N-terminal amino acid sequences revealed that several NoVBPs are relatives to a chaperonine protein, GroEL, which can interact with denatured hydrophobic proteins. The NoVBPs recovered in this study might be useful as versatile adsorbents for norovirus recovery or detection from environmental water samples.
2007-12-10