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Infect Immun. 1991 December; 59(12): 4473-4477

Blocking of fimbria-mediated adherence of Haemophilus influenzae by sialyl gangliosides.

L van Alphen, L Geelen-van den Broek, L Blaas, M van Ham and J Dankert

Department of Medical Microbiology, University of Amsterdam, The Netherlands.

ABSTRACT

The structure of the receptor for the fimbriae of Haemophilus influenzae on human oropharyngeal epithelial cells and erythrocytes was determined in inhibition experiments with various sugars, glycolipids, and glycoproteins. Of 30 monosaccharides and disaccharides at a concentration of 0.1 M and of 3 polysaccharides at a concentration of 1 mg/ml, none inhibited fimbria-specific adherence and hemagglutination. Inhibition was obtained with gangliosides GM1, GM2, GM3, and GD1a in nanomolar concentrations, whereas the asialo derivative of GM1, sialyl-lactose, and sialoglycoproteins were poor inhibitors. These findings indicate that sialyl-lactosylceramide (GM3) is the minimal structure for the fimbria-dependent binding of H. influenzae to its receptor on oropharyngeal epithelial cells and erythrocytes. As is the case with GM2, substitution of GM3 with N-acetylgalactosamine makes the molecule a 10-fold-better receptor analog.

Infect Immun. 1991 December; 59(12): 4473-4477




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