| Abstract
| - Ovomucin glycopeptide (OGP) was prepared by size exclusion chromatography after Pronasedigestion of hen egg ovomucin, and the binding of OGP to foodborne pathogens (Bacillus cereus,Clostridium perfringens, Escherichia coli O157:H7, Listeria monocytogenes, Salmonella enteritidis,Salmonella typhimurium, and Staphylococcus aureus) was investigaed. Binding assays withbiotinylated bacteria as probes in microtiter plates showed that OGP bound to only E. coli O157:H7among these foodborne pathogens. Periodate treatment markedly reduced the binding ability,indicating that E. coli O157:H7 bound to carbohydrate moieties of OGP. Lectin blot analysis withMaackia amurensis (MAA) and Sambucus nigra (SNA), which are specific for oligosaccharidescontaining sialic acid, revealed their binding sites in OGP were similar to the E. coli O157:H7 bindingsites that were probed with biotinylated E. coli O157:H7 after Western blotting of OGP. Sialydasetreatment of OGP abolished its ability to bind E. coli O157:H7, demonstrating that sialic acid playedan important role in the binding. These results suggest that OGP has E. coli O157:H7-specific bindingsites that consist of sialic acid. On the basis of these properties, OGP has the potential to be aningredient with a protective effect against E. coli O157:H7 infection and to be a novel probe for thedetection of E. coli O157:H7 in the food hygiene field. Keywords: Ovomucin; glycopeptide; foodborne illness; Escherichia coli O157:H7; sialic acid; bacterialadhesion
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