Chemoenzymatic synthesis of ?2-3-sialylated carbohydrate epitopes.

ABSTRACT: Sialic acids are common terminal carbohydrates on cell surface. Together with internal carbohydrate structures, they play important roles in many physiological and pathological processes. In order to obtain ?2-3-sialylated oligosaccharides, a highly efficient one-pot three-enzyme synthetic approach was applied. The P. multocida ?2-3-sialyltransferase (PmST1) involved in the synthesis was a multifunctional enzyme with extremely flexible donor and acceptor substrate specificities. Sialyltransferase acceptors, including type 1 structure (Gal?1-3GlcNAc?ProN(3)), type 2 structures (Gal?1-4GlcNAc?ProN(3) and 6-sulfo-Gal?1-4GlcNAc?ProN(3)), type 4 structure (Gal?1-3GalNAc?ProN(3)), type 3 or core 1 structure (Gal?1-3GalNAc?ProN(3)) and human milk oligosaccharide or lipooligosaccharide lacto-N-tetraose (LNT) (Gal?1-3GlcNAc?1-3Gal?1-4Glc?ProN(3)), were chemically synthesized. They were then used in one-pot three-enzyme reactions with sialic acid precursor ManNAc or ManNGc, to synthesize a library of natural occurring ?2-3-linked sialosides with different internal sugar units. The sialylated oligosaccharides obtained are valuable probes for their biological studies.

SUBMITTER: Shengshu H 

PROVIDER: S-EPMC3115702 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature