Adhesion of viridans group streptococci to sialic acid-, galactose- and N-acetylgalactosamine-containing receptors

The binding of 10 viridans group streptococci to sialic acid-, galactose (Gal)- and N-acetylgalactosamine (Ga1NAc)-containing receptors was defined by analysis of the interactions between these bacteria and structurally defined glycoconjugates, host cells and other streptococci. All interactions with sialic acid-containing receptors were Ca²⁺-independent as they were not affected by ethyleneglycoltetraacetic acid (EGTA), whereas all interactions with Gal- and GalNAc-containing receptors were Ca²⁺-dependent. Recognition of sialic acid-, Gal- and Ga1NAc-containing receptors varied widely among the strains examined, in a manner consistent with the association of each of the three lectin-like activities with a different bacterial cell surface component.