1887

Abstract

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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1996-05-01
2021-08-02
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