Nonimmunoglobulin fraction of human milk inhibits bacterial adhesion (hemagglutination) and enterotoxin binding of Escherichia coli and Vibrio cholerae.
Human milk and colostrum samples were divided into an immunoglobulin and a nonimmunoglobulin fraction by immunosorbent chromatography. The ability of these fractions to inhibit bacterial cell adhesion and enterotoxin receptor binding of Vibrio cholerae and various Escherichia coli isolates was then tested by in vitro assays. The strongest effect was generally seen with the nonimmunoglobulin fractions, which were shown to significantly inhibit E. coli cell adhesion (hemagglutination) mediated by CFA/I, CFA/II, or K88 fimbriae (but not type 1 pili) and V. cholerae hemagglutination, as well as the binding of cholera toxin and E. coli heat-labile enterotoxin to GM1 ganglioside. Also, the immunoglobulin fractions had significant inhibitory activity in some of these systems. The results are interpreted to suggest that human milk and colostrum may contain secreted structure analogs of the cell receptors for some bacterial adhesions and enterotoxins; this might contribute to the protective effect of milk against enteric infections.
D018407:Bacterial Physiological Phenomena; D001427:Bacterial Toxins; D002772:Cholera Toxin / Q000378:metabolism; D003126:Colostrum / Q000502:physiology*; D004768:Enterotoxins / Q000378:metabolism*; D004926:Escherichia coli / Q000502:physiology; D029968:Escherichia coli Proteins; D005677:G(M1) Ganglioside / Q000378:metabolism; D006384:Hemagglutination; D006801:Humans; D007136:Immunoglobulins / Q000494:pharmacology; D008895:Milk, Human / Q000502:physiology*; D014734:Vibrio cholerae / Q000502:physiology
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D007136:Immunoglobulins; D005677:G(M1) Ganglioside; D002772:Cholera Toxin; C027538:heat-labile enterotoxin, E coli