Novel cell‐binding activity specific for N‐acetyl‐D‐glucosamine in an Escherichia coli strain

FEBS Letters

Korhonen, Timo K.¹  Finne, Jukka²  Väisänen-Rhen, Vuokko¹ 

[1] Department of General Microbiology, University of Helsinki, Siltavuorenpenger 10, SF-00170 Helsinki 17, Finland;Department of Medical Chemistry, University of Helsinki, Siltavuorenpenger 10, SF-00170 Helsinki 17, Finland

关键词: N-Acetyl-D-glucosamine;    Bacterial adhesion;    Endo-β-galactosidase;    Erythrocyte;    Haemagglutination;    Receptor;   

DOI  :  10.1016/0014-5793(83)80453-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Escherichia coli strains isolated from patients with different levels of urinary tract infection and from healthy persons were tested for their ability to haemagglutinate endo-β-galactosidase-treated human erythrocytes. Among the 104 strains studied one revealed a strong agglutination reaction with the enzyme-treated erythrocytes. From the monosaccharides tested N-acetyl-D-glucosamine inhibited agglutination most effectively. Orosomucoid and asialo-orosomucoid had no effect on the haemagglutination whereas β-galactosidase treated asialo-orosomucoid was inhibitory. These findings indicate that the E. coli strain studied contains a novel cell-binding activity with specificity for terminal N-acetyl-D-glucosamine residues.

【 授权许可】

Unknown