Nine strains of isolated from blood cultures of patients with infective endocarditis or from the oral cavity as part of the normal flora, were examined for their ability to elaborate sialidase (neuraminidase) and -acetylglucosaminidase, enzymes which are involved in the degradation of glycoproteins. Both glycosidases were induced when bacteria were grown in a minimal medium supplemented with porcine gastric mucin, a model glycoprotein, and repressed when growth occurred in the presence of glucose. Cell-free extracts of mucin-grown cultures expressed elevated levels of -acetylneuraminate pyruvate-lyase (the first intracellular enzyme in the pathway of -acetylneuraminate catabolism), acetylglucosamine (GlcNAc)-6-phosphate deacetylase and glucosamine-6-phosphate deaminase (enzymes involved in the intracellular catabolism of GlcNAc 6-phosphate); activity of each of these intracellular enzymes was markedly repressed when bacteria were grown in the presence of glucose. Three strains of were also grown in media supplemented with α-acid glycoprotein, a major component of human plasma. Cells from these cultures expressed high levels of sialidase, -acetylglucosaminidase, and the intracellular enzymes involved in the catabolism of -acetyl-sugars released by the action of these glycosidases. High-resolution H-NMR spectroscopy of spent culture supernatants revealed that sialic acid and GlcNAc residues of the molecularly mobile oligosaccharide side-chains of α-acid glycoprotein had been hydrolysed and the released sugars internalized by the bacteria. These data indicate that has the ability to hydrolyse constituents of oligosaccharide side-chains of host-derived glycoproteins and to utilize simultaneously these released carbohydrates. The biochemical characteristics induced by the growth of on glycoproteins may play a role in the survival and persistence of these bacteria at the infection site


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