Enzymatic synthesis of a 6′-sulphated sialyl-Lewisx which is an inhibitor of L-selectin binding to peripheral addressin

A sulphated form of sialyl-Lewisx, NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc6OSO3β1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3β1-3Gal, using sequential steps involving β1,4-galactosyltransferase, α2,3-trans-sialidase and recombinant α1,3-fucosyltransferase, respectively. Su...

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Bibliographic Details
Published in:Glycobiology (Oxford) 1994-12, Vol.4 (6), p.929-932
Main Authors: Scudder, Peter R., Shailubhai, Kunwar, Duffin, Kevin L., Streeter, Philip R., Jacob, Gary S.
Format: Article
Language:English
Subjects:
Animals
Antigens, Surface - chemistry
Antigens, Surface - metabolism
Carbohydrate Sequence
Cell Adhesion Molecules - metabolism
homing receptor
In Vitro Techniques
L-Selectin
Lewis X Antigen - analogs & derivatives
Ligands
lymphocyte
Mass Spectrometry
Membrane Proteins
Molecular Sequence Data
Oligosaccharides - biosynthesis
Oligosaccharides - chemistry
Oligosaccharides - metabolism
peripheral addressin
sulphated sialyl-Lewisx
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Summary:A sulphated form of sialyl-Lewisx, NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc6OSO3β1-3Gal, was synthesized enzymatically from a precursor disaccharide, GlcNAc6OSO3β1-3Gal, using sequential steps involving β1,4-galactosyltransferase, α2,3-trans-sialidase and recombinant α1,3-fucosyltransferase, respectively. Successful enzymatic fucosylation at the 3 position of the GlcNAc6OSO3 residue demonstrated that fucosyltransferases are capable of generating, in situ, sulphated sialyl Lewisx structures containing sulphate at the 6 position of GlcNAc. The sulphated sialyl-Lewisx pentasaccharide produced by this procedure inhibited binding of a soluble form of L-selectin to 35SO4-labelled peripheral addressin with an IC50 of 0.8 mM, whereas sialyl-Lewisx tetrasaccharide was a weaker inhibitor, displaying an IC50 of 3.2 mM. Hemmerich and Rosen (Biochemistry, 33, 4820–4829, 1994) recently reported the presence of Galβ1-4GlcNAcO6SO3 structures on murine peripheral addressin Sgp50, in addition to sialyl Lewisx structures sulphated at the 6-O-galactose position. Based on our data, we suggest that sialyl Lewisx sulphated at the 6-O-GlcNAc position may also exist on receptors and function as a ligand for L-selectin.
ISSN:0959-6658
1460-2423
DOI:10.1093/glycob/4.6.929