, part of the group’, has the ability to produce glycosaminoglycan depolymerising enzymes (hyaluronidase and chrondroitin sulphate depolymerase) which is unique amongst the viridans streptococci and may contribute to their virulence in brain and liver abscesses. The growth of strain UNS 35 was studied in basal medium supplemented with chondroitin sulphate A (CS-A, sulphated at position 4 of the N-acetylgalactosamine moiety) or chondroitin sulphate C (CS-C, sulphated at position 6 of the N-acetylgalactosamine moiety) as the major carbohydrate source. CS-A but not CS-C supported the growth of Extracellular degradation of CS-A resulted in the initial accumulation of 2-acetamido-2-deoxy-3-O-(β-D-gluco-4-δenepyranosyluronic acid)-D-galactose (δUA GalNAc-0S), and low levels of 2-acetamido-2-deoxy-3-O-(β-D-gluco-4-δenepyranosyl uronic acid)-4-O-sulpho-D-galactose (δUA GalNAc-4S) in the medium with GalNAc-0S being subsequently utilised during bacterial growth. Metabolic end-products included formate and ethanol but not lactate, indicating that growth was probably carbon-limited. The CS-A contained 30% CS-C, which was also depolymerised resulting in the formation of 2-acetamido-2-deoxy-3-O-(β-D-gluco-4-δenepyranosyluronic acid)-6-O-sulpho-D-galactose (δUA GalNAc-6S) in the culture supernate, but this unsaturated disaccharide was apparently not utilised during growth. The results indicate that produced CS-AC depolymerase, which was inducible and extracellular, and sulphatase activity. Experiments with authentic δUA GalNAc-4S and δUA GalNAc-6S demonstrated that δUA GalNAc-4S rather than δUA GalNAc-6S was the preferred substrate for the sulphatase. Therefore, it is suggested that the CS-AC depolymerase of may play a role in the destruction of CS in host tissues, facilitating bacterial spread, and also in bacterial nutrition by the liberation of nutrients at the site of infection.


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