Method for the production of sialylated oligosaccharides

Details Method for the production of sialylated oligosaccharides Method for the production of sialylated oligosaccharides

1998-09-03

2001-02-27

Prats, Francisco (Department: 1651)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Preparing compound containing saccharide radical

C435S101000, C435S072000, C435S074000, C435S097000

Reexamination Certificate

active

06194178

ABSTRACT:

BACKGROUND OF THE INVENTION
1. Field of the Invention
This application is directed to methods for the enzymatic synthesis of &agr;-sialylated oligosaccharides. Specifically, in the methods of this invention &agr;2,3-sialyltransferase is employed to transfer sialic acid or an analogue thereof, employed as its CMP-nucleotide, to the non-reducing terminus of an oligosaccharide which oligosaccharide has a fucosyl group in the position penultimate to the non-reducing sugar terminus of the oligosaccharide.
2. References
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3. State of the Art
Carbohydrates and/or oligosaccharides are present on a variety of natural and pathological glycoconjugates
1
. Of particular interest are carbohydrates and oligosaccharides containing sialic acid residues particularly at the nonreducing sugar terminus
31
Such sialic acid terminated carbohydrates and oligosaccharides are present in a number of products which have been implicated in a wide range of biological phenomena based, in part, on the concept of recognition signals carried by the carbohydrate structures and by their binding to specific ligands.
Specifically, such sialic acid terminated carbohydrates and oligosaccharides are believed to be receptors for the binding of toxins
4
, pathogenic agents such as viruses
5
, and are believed to be recognition sites for a variety of lectins, particularly those involved in cellular adhesion
6,7
, etc.
Similarly, certain oligosaccharides including sialic acid terminated oligosaccharides have been identified as capable of suppressing a cell-mediated immune response to an antigen. The ability of such oligosaccharides to suppress a cell mediated immune response to an antigen is described by Venot et al.
3
Additionally, the presence of certain sialyl terminated oligosaccharides in tumor-related antigens is documented in the art
1
and, in general, the structures of the oligosaccharides present on such antigens have been modified in some way from normal oligosaccharides so as to lead to the expression of tumor related antigens
2
. The prospect of passive immunotherapy with monoclonal antibodies directed against some sialylated tumor-associated antigens, such as the gangliosides GD
2
, GD
3
and GM
2
, in patients with melanoma has been investigated
8,9
.
The synthesis of such oligosaccharides often involves complex chemical reactions with corresponding low yields. Accordingly, there has been much interest in using glycosyltransferases in synthesizing at least a part of these molecules.
Glycosyltransferases are a highly polymorphic group of membrane-bound enzymes of endoplasmic reticulum and Golgi bodies that catalyze the transfer of a single monosaccharide unit from a nucleotide donor to the hydroxyl group of an acceptor saccharide in the biosynthesis of N-glycan (Asn-GlcNAc N-glycosidic linkage; GlcNAc, N-acetylglucosamine) and O-glycan (Ser/Thr-GalNAc, O-glycosidic linkage; GalNAc, N-acetylgalactosamine) moieties of glycoproteins and glycolipids.
The eukaryotic sialyltransferases comprise a family of glycosyltransferases that catalyze the transfer of N-acetylneuraminic acid (NeuAc), a sialic acid (SA), from CMP-SA to the non-reducing terminus of oligosaccharide chains of glycoconjugates. The addition of the sialic acid normally terminates oligosaccharide chain elongation except for polysialic chains found on neural cell adhesion molecule and gangliosides.
Known eukaryotic sialyltransferases involved in the synt

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