1887

Abstract

lectins interact with strains OB and OB, 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 OB by the galactose-binding lectin was inhibited by -galactose and by the lipopolysaccharide extracted from OB. Similarly, the specific agglutination of OB by the mannose-binding lectin (which also binds -fucose, -galactose and -fructose) was inhibited by -mannose, -fucose, -galactose and -fructose, as well as by the lipopolysaccharide extracted from OB. The interaction between OB and the 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 OB lipopolysaccharide.

Treatment of cells of the two strains with protein-denaturing agents did not reduce their agglutination by the 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 lectins interact with the B and H (O) blood group determinant sugars (-galactose in OB and -fucose in OB) residing in the lipopoly-saccharides of these strains.

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/content/journal/micro/10.1099/00221287-123-2-359
1981-04-01
2020-10-24
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-123-2-359
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