Glycopeptides from egg white ovomucin inhibit K88ac enterotoxigenic Escherichia coli adhesion to porcine small intestinal epithelial cell-line

Anti-adhesive therapy is emerging as an alternative approach to antibiotics against bacterial infection. The anti-adhesive activity of ovomucin hydrolysates against K88(ac) enterotoxigenic Escherichia colt (ETEC) strains adhesion to porcine small intestinal epithelial cell-line (IPEC-J2) was confirmed using both the plate counting and Syto 9 staining methods. Ovomucin-protex 26L hydrolysate, with the minimum effective concentration of 2.5 g/L, showed the best anti-adhesive activity. Immunofluorescence assay suggested that ovomucin hydrolysates did not decrease the binding capacity of IPEC-J2 cells to K88 fimbriae. Interactions between ovomucin-protex 26 L hydrolysate and purified K88(ac) fimbriae indicated the anti-adhesive activity of ovomucin hydrolysates was due to their decoying properties for competitive binding to ETEC through K88(ac) fimbriae. The responsible glycopeptides in ovomucin-protex 26 L hydrolysate was purified by affinity chromatography and nine peptide sequences and twelve possible glycans were identified. Ovomucin derived glycopeptides may have the potential for use as an anti-adhesive agent against infectious diseases.