Bovine muc1 inhibits binding of enteric bacteria to caco-2 cells

Parker, Phillip, Sando, Lillian, Pearson, Roger, Kongsuwan, Kritaya, Tellam, Ross L. and Smith, Stuart 2010, Bovine muc1 inhibits binding of enteric bacteria to caco-2 cells, Glycoconjugate journal, vol. 27, no. 1, pp. 89-97, doi: 10.1007/s10719-009-9269-2.

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Title Bovine muc1 inhibits binding of enteric bacteria to caco-2 cells
Author(s) Parker, Phillip
Sando, Lillian
Pearson, Roger
Kongsuwan, Kritaya
Tellam, Ross L.
Smith, Stuart
Journal name Glycoconjugate journal
Volume number 27
Issue number 1
Start page 89
End page 97
Total pages 9
Publisher Springer Netherlands
Place of publication Amsterdam, The Netherlands
Publication date 2010-01
ISSN 0282-0080
Keyword(s) milk mucins
enteric pathogen
adhesion inhibition
Summary Inhibition of bacterial adhesion to intestinal epithelial receptors by the consumption of natural food components is an attractive strategy for the prevention of microbial related gastrointestinal illness. We hypothesised that Muc1, a highly glycosylated mucin present in cows’ milk, may be one such food component. Purified bovine Muc1 was tested for its ability to inhibit binding of common enteric bacterial pathogens to Caco-2 cells grown in vitro. Muc1 caused dose-dependent binding inhibition of Escherichia coli, Salmonella enterica serovar Typhimurium (S. Typhimurium), Staphylococcus aureus and Bacillus subtilis. This inhibition was more pronounced for the Gram negative compared with Gram positive bacteria. It was also demonstrated that Muc1, immobilised on a membrane, bound all these bacterial species in a dose-dependent manner, although there was greater interaction with the Gram negative bacteria. A range of monosaccharides, representative of the Muc1 oligosaccharide composition, were tested for their ability to prevent binding of E. coli and S. Typhimurium to Caco-2 cells. Inhibition was structure dependent with sialic acid, L(-) fucose and D(+) mannose significantly inhibiting binding of both Gram negative species. N-acetylglucosamine and N-acetylgalactosamine significantly inhibited binding of E. coli whilst galactose, one of the most abundant Muc1 monosaccharides, showed the strongest inhibition against S. Typhimurium. Treatment with sialidase significantly decreased the inhibitory properties of Muc1, demonstrating the importance of sialic acid in adhesion inhibition. It is concluded that bovine Muc1 prevents binding of bacteria to human intestinal cells and may have a role in preventing the binding of common enteropathogenic bacteria to human intestinal epithelial surfaces.
Language eng
DOI 10.1007/s10719-009-9269-2
Field of Research 060599 Microbiology not elsewhere classified
090899 Food Sciences not elsewhere classified
100399 Industrial Biotechnology not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2009, Springer Science + Business Media, LLC
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