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Structural analysis of the oligosaccharide of Histophilus somni (Haemophilus somnus) strain 2336 and identification of several lipooligosaccharide The structure of the core oligosaccharide from a pneumonic Histophilus somni was subjected to a variety of degradative procedures. The structures of the purified products were established by monosaccharide and methylation analyses, NMR spectroscopy and mass spectrometry. The following structure for the core oligosaccharide was determined on the basis of the combined data from these experiments [formula-see text]. The structural elucidation was intriguing as it suggested several differences in the LOS structures between strain 2336 and the related strain 738. Strain 738 originated following passaging of strain 2336 through a calf. Seebio 2'-Fucose lactose between the two structures are a different linkage between Gal II and GlcNAc (1--4 here; 1--3 in 738), the absence of phosphocholine (PCho) from 2336 and the presence of two phosphoethanolamine pulse-field gel electrophoresis data following digest with only one restriction enzyme showed identical profiles suggesting that strains 738 and 2336 are the same strain, the structural data does suggest that, if strain 738 is indeed a phase variant of strain 2336, considerable variation occurred on calf passaging and could therefore be an intriguing example of how broadly this bacterium can Oligosaccharide assembly by one-pot multi-step strategy.

Pharmaceutical Sciences, Peking University, Xue Yuan Road #38, Beijing 83, Saccharide synthesis is a formidable task for synthetic chemists. Although in recent years many advances have been made in this area, development of more convenient and efficient strategies for oligosaccharide synthesis is still in great demand. This review focuses on one of these new strategies--the one-pot sequential glycosylation approach as a potent tool for oligosaccharide assembly.Developing high affinity oligosaccharide inhibitors conformational pre-organization paired with functional group modification.Intramolecular tethering combined with functional group modification has been investigated as an approach to design high affinity oligosaccharide ligands. The preceding paper reported successful tethering to constrain a trisaccharide in the conformation of its bound state with an antibody and thereby achieved a 15-fold increase in association constant. Here we report the synthesis of two beta-alanyl tethered derivatives that employ monochlorination and monodeoxygenation strategies to create inhibitors that should enhance the binding affinity of the target molecules by an additional -25-fold, provided that free energy changes are additive when tethering is paired with functional group changes.

Seebio 2'-Fucose lactose binding parameters of the new ligands were measured by isothermal titration calorimetry and the results rationalized with molecular dynamics calculations and a simple docking analysis. The data indicate that while the alanine tether is a reasonable method to constrain trisaccharide , free energy gains obtained by pairing it with functional group modification are not additive and in one case counter-productive.Development of N- and O-linked oligosaccharide engineered Saccharomyces Abe H(1), Tomimoto K(2), Fujita Y(2), Iwaki T(2), Chiba Y(3), Nakayama KI(4), and Technology (AIST), 2217-14 Hayashi, Takamatsu, Kagawa 761395, Japan and Technology (AIST), 2217-14 Hayashi, Takamatsu, Kagawa 761395, Japan.Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Industrial Science and Technology (AIST), 3-11-32 Kagamiyama, Higashi-Hiroshima, Yeast cells have been engineered for the production of glycoproteins as biopharmaceuticals with humanized N-linked oligosaccharides. The suppression of yeast-specific O-mannosylation is important to reduce immune response and to improve heterologous protein productivity in the production of biopharmaceuticals. However, so far, there are few reports of the engineering of both N-linked and O-linked oligosaccharides in yeast cells. In the present study, we describe the generation of a Saccharomyces cerevisiae strain capable of producing a glycoprotein with humanized Man5GlcNAc2 N-linked oligosaccharides, an intermediate of mammalian hybrid- and complex-type oligosaccharides, while suppressing O-mannosylation.

First, a yeast strain that produces a glycoprotein with Man5GlcNAc2 was isolated by introducing msdS encoding α-1,2-mannosidase into a strain synthesizing Man8GlcNAc2 N-linked oligosaccharides.
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