Blackwell Publishing Journal Backfiles 1879-2005
Whole-cell affinity chromatography was used as a novel screening technique for identifying and characterizing oral microbial lectins. First, affinity columns bearing oligosaccharides of defined structure were synthesized as lectin-binding reagents. Fetuin, transferrin (containing terminal NeuAc residues), asialofetuin and asialotransferrin (with terminal Gal residues) were covalently coupled to Sepharose 6MB and incubated with 3H-labeled bacterial suspensions in columns fitted with an 80-μm nylon filter. Bacteria specifically bound were then eluted with the appropriate sugar (NeuAc or Gal). Fusobacterium nucleatum was the most significant binder, with 80% specifically eluted from the asialo-derivatives. Actinomyces viscosus and Actinomyces naeslundii also showed unique specificity for galactose. In contrast, Streptococcus sanguis bound in greatest numbers to fetuin, consistent with the presence of a sialic acid-binding site on these bacteria.
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