Lectin-like activity of Escherichia coli K88, Salmonella choleraesuis, and Bifidobacteria pseudolongum of porcine gastrointestinal origin.

The lectin-like activity of Escherichia coli K88, Salmonella choleraesuis, and Bifidobacteria pseudolongum of porcine gastrointestinal origin was studied by hemagglutination (HA) and HA inhibition assays. Although all the bacterial strains were able to agglutinate Porcine and Lagomorpna erythrocytes, much higher HA titers were consistently observed for B. pseudolongum than for E. coli K88 or S. choleraesuis. Proteinaceous components and glycoproteins were responsible for the HA of E. coli K88 and B. pseudolongum, respectively, because a remarkable reduction of HA titers occurred due to treatment of E. coli K88 with protease or trypsin and of B. pseudolongum with protease and periodate. Hemagglutination of E. coli K88, S. choleraesuis, and B. pseudolongum was strongly inhibited by galactosyl residue-containing glycoproteins, including porcine and bovine mucin, thyroglobulin, and fetuin. Some sugars, including lactose, galactose, xylose, and xylooligosaccharide (XOS), at a relatively high concentration (47 to 92 mg/mL) also exhibited an inhibitory activity for the HA of B. pseudolongum. This result, combined with the enhanced HA activity of the three bacterial strains by modification of Lagomorpna erythrocytes with neuraminidase, indicated that galactosyl residue-containing glycoproteins mediated the HA of E. coli K88, S. choleraesuis, and B. pseudolongum. Our study demonstrated that proteinaceous or glycoproteinaceous lectin-like substances that recognize galactosyl residue-containing molecules, especially intestinal mucin, exist on the surface of E. coli K88, S. choleraesuis, and B. pseudolongum.