Trypanosoma cruzi trans-sialidase. A tool for the synthesis of sialylated oligosaccharides

Cells are covered by a complex array of carbohydrates. Among them, sialosides are of key importance in intracellular adhesion, recognition and signaling. The need for structurally diverse sialosides impelled the search for efficient synthetic methods since their isolation from natural sources is a difficult task. The enzymatic approach obviates the need of a chemical synthesis for protecting or participating groups in the substrates. The trans-sialidase of Trypanosoma cruzi (TcTS) is highly stereospecific for the transfer of sialic acid from an α-sialylglycoside donor to a terminal β-galactopyranosyl unit in the acceptor substrate to form the α-Neu5Ac-(2 → 3)-β-D-Galp motif. The enzyme was cloned and easily available glycoproteins, e.g. fetuin, may be used as donors of sialic acid, constituting strong points for the scalability of TcTS–catalyzed reactions. This review outlines the preparative use of TcTS for the sialylation of oligosaccharides. A detailed description of the substrates used as sialic acid donors, the acceptor substrates and the methods employed to monitor the reaction is included. [Display omitted] •Sialosides play a crucial role in cellular recognition events.•TcTS transfers sialic acid from a sialylglycoside to form α-Neu5Ac-(2 → 3)-β-Galp•Enzymatic sialylation can be monitored by chromatography, NMR or mass spectroscopy.•The synthesis of sialyloligosaccharides by preparative TcTS reactions is reviewed.