Inhibition of adhesion of S-fimbriated Escherichia coli to buccal epithelial cells by human milk fat globule membrane components: a novel aspect of the protective function of mucins in the nonimmunoglobulin fraction
| Autor: | G Uhlenbruck, V. Wahn, J Hacker, F G Hanisch, R. Nobis-Bosch, Horst Schroten, R Plogmann |
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| Rok vydání: | 1992 |
| Předmět: |
Immunology
Fimbria Blotting Western Neuraminidase medicine.disease_cause Microbiology Bacterial Adhesion Epithelium Feces medicine Escherichia coli Glycophorin Humans Glycophorins chemistry.chemical_classification Membranes biology Milk Human Colostrum Mucin Infant Newborn Mucins Orosomucoid Milk Proteins Fetuin Agglutination (biology) Infectious Diseases chemistry Fimbriae Bacterial biology.protein Parasitology alpha-Fetoproteins Glycoprotein Research Article |
| Zdroj: | Infection and immunity. 60(7) |
| ISSN: | 0019-9567 |
| Popis: | We investigated the presence of factors in human milk that inhibit invasion of pathogenic bacteria. The effect of human milk fat globule membrane (HMFGM) components on adhesion of cloned S-fimbriated Escherichia coli to human buccal epithelial cells was analyzed. S fimbriae are a common feature of E. coli strains causing sepsis and meningitis in newborns and are bound to epithelia via sialyl-(alpha-2-3)galactoside structures. Human milk fat globules (HMFG) could be agglutinated by the above-mentioned bacteria. Agglutination could be inhibited by fetuin, human glycophorin, and alpha 1-acid glycoprotein. In addition, pretreatment of HMFG with Vibrio cholerae neuraminidase markedly reduced bacterium-induced agglutinations, indicating the involvement of neuraminic acid-containing glycoproteins. In contrast, lipid droplets of infant formula or artificial lipid emulsions (Intralipid) could not be agglutinated. HMFG were present in stools of breast-fed neonates as shown by indirect immunofluorescence staining with a monoclonal antibody directed against carbohydrate residues present on HMFGM. These HMFG could be agglutinated by bacteria. HMFG inhibited E. coli adhesion to buccal epithelial cells. To further characterize relevant E. coli binding structures, HMFGM components were separated by gel chromatography. The mucin fraction showed the most pronounced inhibitory effect on adhesion of S-fimbriated E. coli to human buccal epithelial cells. Our data suggest that HMFG inhibit bacterial adhesion in the entire intestine and thereby may provide protection against bacterial infection. |
| Databáze: | OpenAIRE |
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