Depolymerization-Streptococcus-Pneumoniae-Type-Polysaccharide-w

2'-fucosyllactose (1), Zhang J(1), Zhu H(1), Wang M(2), Polizzi SJ(3), Jones MT(2), Li L(1), Pfizer, Inc., 875 Chesterfield Parkway West, Chesterfield, MO, 617, United Pfizer, Inc., 875 Chesterfield Parkway West, Chesterfield, MO, 617, United Although there have been decades of research on streptococcus pneumoniae, it is still among the leading cause of infectious disease in the world. As a type of capsular polysaccharide (CPS) of streptococcus pneumoniae, pneumococcal polysaccharides are essential components for colonization and virulence in mammalian hosts. This study aimed to characterize the CPS structure of type 8 streptococcus pneumoniae, which is one of the most fatal serotypes. In this work, heparinase I&III was used to successfully digest pneumococcal type 8 polysaccharide (Pn8P).

We characterized the oligosaccharide generated from the enzymatic depolymerization of Pn8P by size exclusion chromatography, mass spectrometry and nuclear magnetic resonance. This is the first study to enzymatically depolymerize and characterize Pn8P.Recent development of phosphorylases possessing large potential for Phosphorylases are one group of carbohydrate active enzymes involved in the cleavage and formation of glycosidic linkages together with glycoside hydrolases and sugar nucleotide-dependent glycosyltransferases. Noticeably, the catalyzed phosphorolysis is reversible, making phosphorylases suitable catalysts for efficient synthesis of particular oligosaccharides from a donor sugar 1-phosphate and suitable carbohydrate acceptors with strict regioselectivity. Although utilization of phosphorylases for oligosaccharide synthesis has been limited because only few different enzymes are known, recently the number of reported phosphorylases has gradually increased, providing the variation making these enzymes useful tools for efficient synthesis of diverse oligosaccharides.High resolution of oligosaccharide mixtures by ultrahigh voltage micellar electrokinetic capillary chromatography.Oligosaccharide mixtures released from ribonuclease B and human IgG have been separated using micellar electrokinetic capillary chromatography operated at 0 kV.

The resolution of these closely related analytes at this high voltage was found to be superior to that obtained at kV, a voltage which is ordinarily used in most capillary electrophoresis separations.Sequence-selective carbohydrate-DNA interaction dimeric and monomeric forms of the calicheamicin oligosaccharide interfere with transcription factor function.Liu C(1), Smith BM, Ajito K, Komatsu H, Gomez-Paloma L, Li T, Theodorakis EA, The synthetic oligosaccharide moiety of the antibiotic calicheamicin and the head-to-head dimer of this oligosaccharide are known to bind to the minor groove of DNA in a sequence-selective manner preferring distinct target sequences. We tested these carbohydrates for their ability to interfere with transcription factor function. 2'-fucosyllactose inhibit binding of transcription factors to DNA in a sequence-selective manner, probably by inducing a conformational change in DNA structure. They also interfere with transcription by polymerase II in vitro. The effective concentrations of the oligosaccharides for inhibition of transcription factor binding and for transcriptional inhibition are in the micromolar range.

The dimer is a significantly more active inhibitor than is the [Oligosaccharide sulfate inhibitors of selectin-sugar interactions in Leucocyte migration into lymphatic tissues or inflammatory sites depends upon the expression of adhesion molecules. Among these molecules, the selectins expressed on endothelial cells (E- and P-selectins) and leucocytes (L-selectin) recognize carbohydrate ligands such as sialyl Lewis A or sialyl Lewis X oligosaccharides due to the same positioning of NeuAc, Gal and Fuc residues in both isomeric structures. We have shown that the sialic acid residue could be replaced by a sulfate group such as in the sulfated Lewis A pentasaccharide, one of the most potent monovalent ligand for human E-selectin, which was shown to be very active in the prevention of ischemia reperfusion lung injury. In the same way, we have prepared through chemoenzymatic syntheses, two disulfated Lewis X pentasaccharides, the sulfated analogs of carbohydrate ligands found on GLYCAM 1, the natural receptor of L-selectin. Finally, based on the double recognition of L-selectin with Lewis type and glycosaminoglycan structures, we tentatively introduced a possible link between the selectin- and the integrin-mediated Genetic tailoring of N-linked oligosaccharides the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo.