%0 Journal Article %A Garber, N. %A Glick, J. %A Gilboa-Garber, N. %A Heller, A. %T Interactions of Pseudomonas aeruginosa Lectins with Escherichia coli Strains Bearing Blood Group Determinants %D 1981 %J Microbiology, %V 123 %N 2 %P 359-363 %@ 1465-2080 %R https://doi.org/10.1099/00221287-123-2-359 %I Microbiology Society, %X Pseudomonas aeruginosa lectins interact with Escherichia coli strains O86B7 and O128B12, which possess B and H (O) blood group determinants, respectively. The interaction could be demonstrated by specific agglutination of the bacteria, by haemagglutination inhibition tests and by lectin-mediated peroxidase binding to the bacteria. The agglutination of E. coli O86B7 by the Pseudomonas galactose-binding lectin was inhibited by d-galactose and by the lipopolysaccharide extracted from E. coli O86B7. Similarly, the specific agglutination of E. coli O128B12 by the Pseudomonas mannose-binding lectin (which also binds l-fucose, l-galactose and d-fructose) was inhibited by d-mannose, l-fucose, l-galactose and d-fructose, as well as by the lipopolysaccharide extracted from E. coli O128B12. The interaction between E. coli O128B12 and the Pseudomonas mannose-binding lectin was also demonstrated by lectin-mediated peroxidase binding to the bacterial surface. Peroxidase binding was also inhibited by the above-mentioned sugars and E. coli O128B12 lipopolysaccharide. Treatment of cells of the two E. coli strains with protein-denaturing agents did not reduce their agglutination by the Pseudomonas lectins. On the other hand, oxidation of the cell surface sugars by sodium metaperiodate or boiling the cells in the presence of 1 % acetic acid for 1 h abolished their agglutination by the two lectins. It is, therefore, suggested that the Pseudomonas lectins interact with the B and H (O) blood group determinant sugars (d-galactose in E. coli O86B7 and l-fucose in E. coli O128B12) residing in the lipopoly-saccharides of these E. coli strains. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-123-2-359