C-glycosyl compounds bind to receptors on the surface of Escherichia coli and can target proteins to the organism

✍ Scribed by Carolyn Bertozzi; Mark Bednarski

• Publisher: Elsevier Science
• Year: 1992
• Tongue: English
• Weight: 881 KB
• Volume: 223
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(92)80021-r

✦ Synopsis

A series of C-mannopyranosyl derivatives have been synthesized and their inhibitory activity towards the receptor-mediated adhesion of E. coli to yeast cells has been tested. Total inhibition of yeast-cell agglutination by C-glycosyl derivatives 4 and 9 is achieved at a concentration approximately one order of magnitude lower than that of methyl alpha-D-mannopyranoside, indicating that the binding affinity to the receptor is related to the hydrophobicity of the carbon-linked side chain. A biotin-linked C-glycosyl derivative of mannose (compound 9) has been synthesized and used to target avidin and streptavidin to the bacterial cell surface. Of the C-glycosyl derivatives tested in our study, the conjugate of compound 9 with avidin had the highest avidity for the bacterial receptors, inhibiting agglutination at a concentration three orders of magnitude lower than methyl alpha-D-mannopyranoside. The use of such bifunctional compounds as the mannose-biotin conjugate 9 is a general strategy to target molecules to pathogenic organisms via their cell-surface carbohydrate receptors and to change the antigenicity of the bacterial cell surface.