Tumor associated carbohydrate antigens (TACAs) are potential cancer vaccine candidates. Recent investigations show that unnatural analogs of these TACAs may have increased immunogenic properties. Sialic acids are terminal monosaccharides of many TACAs, making them important synthetic targets. N-Glycolylneuraminic acid (Neu5Gc) is a non-human sialic acid form which has been found to be presented on certain types of cancer cells and at a lower level in some normal cells. Here we report the cloning and characterization of a human sialyltransferase ST6GalNAc I which has been expressed in Escherichia coli BL21 (DE3). The substrate specificity of the enzymes is also presented. The enzyme can be used in chemoenzymetic synthesis of sialyl-Tn (Siaa2,6GalNAc-O-Ser/Thr) antigens containing natural and unnatural sialic acid derivatives.

Cloning, expression, and characterization of a recombinant human sialyltransferase ST6GalNAc I

239th National Meeting (2010)

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