Bovine Muc1 inhibits binding of enteric bacteria to Caco-2 cells.
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.
Parker
Phillip
P
Faculty of Health, Medicine, Nursing and Behavioural Sciences, School of Exercise and Nutrition Sciences, Deakin University, 221 Burwood Highway, Burwood, 3125, Victoria, Australia. phillip.parker@deakin.edu.au
Sando
Lillian
L
Pearson
Roger
R
Kongsuwan
Kritaya
K
Tellam
Ross L
RL
Smith
Stuart
S
D000818:Animals; D001422:Bacterial Adhesion / Q000187:drug effects; D019921:Biotinylation / Q000187:drug effects; D018938:Caco-2 Cells; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004755:Enterobacteriaceae / Q000187:drug effects / Q000378:metabolism*; D004847:Epithelial Cells / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D055767:Immobilized Proteins / Q000378:metabolism; D008567:Membranes, Artificial; D009005:Monosaccharides / Q000494:pharmacology; D018396:Mucin-1 / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D009439:Neuraminidase / Q000378:metabolism; D011145:Polyvinyls; D005465:Fluorocarbon Polymers
D055767:Immobilized Proteins; D008567:Membranes, Artificial; D009005:Monosaccharides; D018396:Mucin-1; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase; D011145:Polyvinyls; C024865:polyvinylidene fluoride; D005465:Fluorocarbon Polymers