Haataja S, Zhang Z, Tikkanen K, Magnusson G, Finne J
Department of Medical Biochemistry, University of Turku, Finland.
Glycoconj J. 1999 Jan;16(1):67-71. doi: 10.1023/a:1006905904544.
Streptococcus suis causes meningitis and other serious infections in pigs and humans, and binds to host cell globotriosylceramide. In order to determine the essential hydroxyls involved in binding, the complete set of monodeoxy derivatives of the receptor trisaccharide Gal alpha1-Gal beta1-4Glc were tested as inhibitors of bacterial hemagglutination. Removal of the 4''-, 6'', 2' or 3'-hydroxyls abolished inhibitory activity, which indicated that they were critically involved in binding. The same results were obtained using synthetic lipid-linked monodeoxy derivatives of the trisaccharides in a thin-layer overlay assay. The P(N) and P(O) subtypes of the S. suis adhesin showed similar binding patterns. The hydroxyls of the glucose moiety were not critical for binding, although the adhesin binds better to the trisaccharide Gal alpha1-4Gal beta1-4Glc than the disaccharide Gal alpha1-4Gal.
