Chemoenzymatic synthesis of sialyl oligosaccharides with sialidases employing transglycosylation methodology

A series of sialyloligosaccharides was synthesized using the transglycolytic activity of the sialidases from Vibrio cholerae, Clostridium perfringens, Salmonella typhimurium, and Newcastle disease virus. According to their hydrolytic activities the sialidases from V. cholerae and C. perfringens catalyze preferentially the formation of sialyl alpha (2-6)-linkages whereas the sialidases from S. typhimurium and Newcastle disease virus show a distinct preference for alpha (2-3) directed sialylations. Using combined chemical and enzymatic methodologies structures such as T-(Thomsen-Friedenreich) antigen [beta -D-Gal(1-3)-alpha -D-GalNAc-OThr], Tn-(Thomsen nouveau) antigen (alpha -D-GalNAc-OThr) and beta -D-Gal-(1-4)-alpha -D-2-deoxy-Gal-OMe were sialylated in alpha (2-3)- and alpha (2-6)-positions regioselectively or in high regioisomeric excess and purified by simple isolation procedures. Depending on the enzyme source and acceptor structure yields for transsialylation varied between 10 and 30%.