Adsorption characteristics of an enteric virus-binding protein to norovirus, rotavirus and poliovirus

Abstract

BackgroundWater contamination with human enteric viruses has posed human health risks all over the world. Reasonable and facile methodologies for recovering and quantifying infectious enteric viruses in environmental samples are needed to address the issues of waterborne viral infectious diseases. In this study, a bacterial protein that has a binding capability with several enteric viruses is discovered, and its binding characteristics were investigated for utilizing it as a viral adsorbent in virus recovery and detection technologies.ResultsA gene of an enteric virus-binding protein (EVBP), derived from a monomer of a bacterial chaperon protein GroEL, was successfully acquired from a genomic DNA library of activated sludge microorganisms with nested PCR. Equilibrium dissociation constants between EVBP and norovirus-like particles (NoVLPs) of genotypes GI.7 and GII.4, estimated with quartz crystal microbalance method, were 240 and 210 nM, respectively. These values of equilibrium dissociation constant imply that the binding affinity between EVBP and NoVLPs is 1 to 3-log weaker than that in general antigen-antibody interactions, but about 2-log stronger than that in weak specific interactions of proteins with cations and organic polymers. The adsorptions of EVBP to norovirus, group A rotavirus and poliovirus type 1 were found to be significant in enzyme-linked immunosorbent assay. Meanwhile, the binding of native GroEL tetradecamer to viral particles was weaker than that of EVBP, presumably because of a steric hindrance. The small molecule of EVBP could have an advantage in the access to the surface of viral particles with rugged structure.ConclusionsEVBP that has a broad binding spectrum to enteric viruses was newly discovered. The broad binding characteristic of EVBP would allow us to utilize it as a novel adsorbent for detecting diverse enteric viruses in clinical and environmental samples.

Specific Interactions between Human Norovirus and Environmental Matrices: Effects on the Virus Ecology

“…In addition to HBGAs, human norovirus has shown to attach to heparan sulphate [43], sialylated glycans [44], virus binding proteins recovered from activated sludge [45,46], and norovirus attachment proteins in mammalian cells [47]. A study by Gandhi et al [48] reported specific binding of GI to the surface of romaine lettuce, cilantro, and iceberg lettuce via non-HBGA receptors which are not characterized yet.…”

Development of a Portable Detection Method for Enteric Viruses from Ambient Air and Its Application to a Wastewater Treatment Plant

“…The tendency for the transportation of the virus from the aqueous phase to air is unclear on the laboratory scale. The previous study showed that the hydrophobicity of the enteric viruses was different among species [20]. The hydrophobic particles are more likely to be aerosolized (transported to air–water interfaces).…”

The Effect of GD1a Ganglioside-Expressing Bacterial Strains on Murine Norovirus Infectivity

“…In fact, in addition to the MNV that we used in the present study, GD1a ganglioside also takes part in the specific binding of adenovirus, polyomavirus, and porcine sapovirus [ 64 , 76 , 77 ]. Specific virus binding substances have also been proposed to improve virus recovery from and detection in environmental water samples, which have long been impeded by various factors such as low initial concentrations and the presence of inhibitory substances [ 47 ].…”

“…The most studied glycan receptor to date is histo-blood group antigens (HBGAs), a series of complex carbohydrates that can be found on mucosal epithelial cells or in secretions such as the blood and saliva as free antigens, which can be recognized and utilized by human norovirus strains for the infection process in a genotype-specific manner [ 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 ]. Other than HBGAs, specific virus-binding proteins [ 47 , 48 ], heparan sulfate proteoglycan [ 49 ], and sialic acid (SA) linked to glycoproteins and gangliosides [ 11 ] are also known to support the infection processes of a wide spectrum of viruses [ 41 , 45 , 50 ]. Murine norovirus 1 (MNV-1), for instance, recognizes terminal SA moieties in GD1a ganglioside to infect murine macrophages [ 51 ].…”